1. Where can errors in the process of translation occur? 2. Is there an upper and lower limit to the size of the proteins formed? 3. What is AMP and what does it do?
To answer your third question, AMP is a form of ATP with only a single phosphate (adenosine mono phosphate). It is the nucleotide for adenine and also is used to be combined with natural phosphate to create ADP and then ATP.
For your second question, there is not a biological limit, but the smallest protein found was extracted from Gila monsters and consists of 20 amino acids. The largest found is titan which consists of 27000 amino acids.
To answer your third question, I found that AMP is adenosine monophosphate. This is very important for molecules that participate in energy processes in a living cell. Here is a website that explains this further: https://www.britannica.com/science/adenosine-monophosphate
To answer your first question, when eukaryotic cells are exposed to E. coli, mis-translation can occur. An example of this is arginine to lysine substitution, where the arginine rare codon AGA is erroneously recognized by the tRNA that codes for lysine (UUU). More information can be found here: https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5491249/
It is also possible for ribosomes to read through stop codons or have premature termination. More information about this can be found here: https://www.cell.com/trends/genetics/pdf/S0168-9525(17)30227-5.pdf
1. What techniques and technology is used to predict the folding patterns of protein? 2. What are evolutionary precursors to ribasomes? 3. What is a theory for how Ribosomes evolved?
For your first question the most common methods used to prdict proteins structure is x-ray crystallography and nuclear magnetic resonance. More on this can be found here: https://www.sciencedirect.com/topics/biochemistry-genetics-and-molecular-biology/protein-structure-prediction#:~:text=Currently%2C%20the%20main%20techniques%20used,structure%20of%20protein%20is%20determined.
To answer your second question, I could not find a specific name for a precursor, however, what I found was that all ribosomes share the same base components and it is believed that this commonality is what ribosomes originally were. https://astrobiology.nasa.gov/news/the-ribosome-a-record-of-evolution/
In response to your third question, this site goes into great detail on how ribosomes evolved throughout the years. I'd give a description, but I am lazy. https://www.pnas.org/content/112/50/15396
1. How does the structure of proteins change between tertiary and quaternary structure? 2. How do proteins find their way to the location that they are meant to function in? How long does it take for proteins to get to their final form after translation?
To answer your first question, the difference between the tertiary and quaternary structures are that the quaternary structure is multiple polypeptides whereas the tertiary structure is one polypeptide.
In response to your third question, the amount of time it takes for a protein to fold difficult to determine. Often times it will take place in the span of a second, however, the Levinthal Paradox is a result of protein folding. The paradox is that there are many non-native configurations that are unnecessary in the protein folding that would slow the process down for an unknowable period of time. So, there is no specific measurement of the amount of time it takes a protein to fold after translation.
1. Is the space inside a ribosome open or are there compartments/dividers between the 3 binding sites? 2. What is the use of AMP that is released from the enzyme that attaches the amino acid to tRNA? 3. Does the tRNA need to interact with the tRNA-activating enzyme for the 3 stop codons?
For your first question, although some of the diagrams we've used make it appear as if there were clear divides between the binding sites, this is usually to show a simplified version which is easy to understand. The process of translocation makes it impossible for there to be compartments here. The part of the amino acids facing away from the ribosome are first pulled to their new site, creating diagonal location, then the bottoms are transferred. The two amino acids which are transferred remain attached to each other, so they can't move trough compartments without a more advanced process. https://www.pnas.org/content/104/50/19671
To answer your second question, AMP is simply the biproduct of releasing the phosphate from the ADP used by the enzyme. It's main use is to recombine with another phosphate to form ADP and then ATP.
To answer your third question, because there is no tRNA that codes for a stop codon, when the ribosome reaches the stop codon, there is no tRNA that needs to be activated by the tRNA-activating enzyme. Source: https://www.nature.com/scitable/definition/translation-rna-translation-173/
1. what happens in Eukaryotic cells after translation? 2. Why does translation take place in the cytoplasm? 3. How long does it take for elongation to occur?
In response to your third question, the amount of time it takes for elongation depends on the length of the mRNA being translated. However, it is also known that 20 amino acids can be added per second or 60 nucleotides translated per second. So, assuming you know the length of the mRNA being translated or the polypeptide, you can determine about how long it will take for elongation to occur.
To answer your first question, once translation is complete, the completed polypeptides go on to their specific locations and continue to undergo modifications in order to fulfill their shapes and functions as proteins. Signal sequences are the amino acid sequences that direct the polypeptide to its ultimate destination in the body (with the help of other cellular factors). This sequence is then cut off when the protein reaches its location. Proteins destined for the cytoplasm, mitochondria, or chloroplast in plants stay within the cell. Proteins bound for outside the cell are synthesized on ribosomes on the ER and are prepared for secretion at the end of translation. The proteins then start folding into the best structure for their specific function. Sometimes molecules called chaperones are required to prevent error. I hope that this answers at least part of your question! https://courses.lumenlearning.com/suny-wmopen-biology1/chapter/translation/
1) Does a polypeptide’s attachment change from tRNA molecule to tRNA molecule (since one is always leaving from the E site and the polypeptide can't leave the ribosome until the stop codon is reached)? If so, how does this transfer occur? 2) I am a bit confused on how tRNA activating enzymes work. Does this process of attaching an amino acid to the tRNA happen inside the ribosome (while the anticodon is paired with the mRNA codon), or happen outside of the cell first and then the tRNA with the amino acid attaches to the codon via its anticodon? 3) The textbook says that the signal sequence is the first part of the polypeptide translated. Does this mean that the signal sequence occurs before the start codon, or that it is the first codon following?
In response to your second question, the tRNA-activating enzymes are in the cytoplasm and each one has a specific amino acid that binds to it. The enzymes will find tRNA and then bind the amino acid to the tRNA . Once this has been done, the bonded tRNA is released into the cell to attach to ribosomes and participate in the translation process.
To answer your first question, yes the amino acid does go from tRNA to tRNA when in the ribosome. This happens between the tRNA in the E and A site. A peptide bond is formed between the amino acids and the amino acid breaks off from the P site tRNA. The tRNA then move down and the polypeptide chain is now in the same place as before. This goes on until the process is done.
To answer your third question, as the process of translation requires the start codon to come first, the signal sequence would be the sequence following the start codon, being the first to be translated after translation begins.
1) Why does a tRNA molecule have to be recharged? 2) Anyone have a mnemonic for remembering the processes of transcription and translation? 3) Are there more types of RNA?
For your third question I found that there are many types of RNA, but the three most well known are mRNA (messenger RNA),tRNA (transfer RNA) and rRNA (ribosomal RNA).There is also small nuclear rna (snRNA), regulatory RNAs, double-stranded RNAs (dsRNA) and many more other types that are used in all different types of cells! Hope this helped :)
To answer your first question, I found this exact situation on bioninja :) "The function of the ATP phosphorylation is to create a high energy bond that is transferred to the tRNA molecule. This stored energy will provide the majority of the energy required for peptide bond formation during translation." https://ib.bioninja.com.au/higher-level/topic-7-nucleic-acids/73-translation/trna-activation.html The ATP helps to form the amino acid-AMP complex, attach the corresponding amino acid to the tRNA, and leave the tRNA molecule with high enough energy for peptide connection between amino acids in the ribosome. It needs to be charged with this energy each time it helps to build a polypeptide in translation. I hope that this helps!
To answer your second question I have one that outlays the general process but its pretty wacky. It’s “Sometimes My Tarantula Exaggerates Lots Except on Tuesdays”. S - SUBUNIT ribosome M - MRNA binds T - TRNA E - ENERGY is used L - LG SUBUNIT is added E - ELONGATION T - TERMINATION I don’t have a source from this but here is an interesting read on the general process. https://www.khanacademy.org/science/biology/gene-expression-central-dogma/translation-polypeptides/a/the-stages-of-translation
For your second question I found that in translation the amino acids stop elongating, or getting added onto, when the stop codon is read my the tRNA. TRNA cannot code the stop codon of the mRNA, the three stop codons being, UAA, UGA or UAG, because there is no anticodon that can be complementary paired with them. In conclusion, the whole process of translation, including the elongation of amino acids, is stopped when the stop codon is translated.
To answer your third question, translation does occur in the same place in both prokaryotes and eukaryotes: the cytoplasm (more specifically in the cytosol in prokaryotes). The difference in translation between the two is that it occurs simultaneously with transcription in prokaryotes, and discontinuously in eukaryotes. This is because eukaryotes are compartmentalized and keep the DNA within the nucleus. It must make post-transcriptional modifications before the MRNA can exit the nucleus, which results in a slower process than prokaryotic cells. Also, the mRNA will in prokaryotes will not be utilizing ribosomes located on the rough ER, as there is none in a prokaryotic cell. I hope that this helps!
1. How are amino acids constructed? 2. Do ribosomes have an exact partner in terms of small to large, or are they independent pieces that can join together with any other piece? 3. What causes the large half of the ribosome to hook on to the smaller half only when mRNA and tRNA are present?
For your third question, the amino acids hooking onto the enzymes are represented by a three-nucleotide sequence or codon along the mRNA molecule. This specializes the amino acids and other molecules with mRNA. For more information, the source that helped me was https://www.nature.com/scitable/topicpage/ribosomes-transcription-and-translation-14120660/#:~:text=Ribosomes%20are%20the%20sites%20in,which%20protein%20synthesis%20takes%20place.&text=Within%20the%20ribosome%2C%20the%20rRNA,RNA%20to%20reflect%20this%20function.
1. How does mRNA know which ribosome to go to? 2. How does an amino acid know which tRNA and activating enzyme is the correct one? 3. Are there instances where a tRNA molecule is malformed? If so, what happens to it?
For your third question, tRNA molecules can be mutated. If this should happen, diseases that are subject in the brain and neurological disorders will be caused. I cannot explain it as in depth, but here is the source I used for this answer, https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6716996/.
For your second question, an amino acid is coded to where it goes to the activating enzyme. It corresponds with the tRNA. For more information, the source I used was https://www.nature.com/scitable/topicpage/ribosomes-transcription-and-translation-14120660/#:~:text=Ribosomes%20are%20the%20sites%20in,which%20protein%20synthesis%20takes%20place.&text=Within%20the%20ribosome%2C%20the%20rRNA,RNA%20to%20reflect%20this%20function.
1. How are the amino acids specialized for the enzyme? 2. Do cells ever create useless proteins? 3. After the proteins are secreted, can they end up in a place where they are not supposed to be? How would this effect the cell if so?
In response to your second question; there are proteins that are thought to be pretty much useless, but they actually perform small tasks that aren't studied as often, such as varying structural purposes. Even the spare DNA bits that get taken off and left behind after the transcription process that never get made into proteins can have uses that are being discovered, such as amplifying gene expression and the development of mutations such as breast cancer and autism. SO in short, I do not believe that there are any proteins or DNA strands that are completely useless. I hope this helps!
To answer your first question, the enzymes have special bonding sites for the energy source, tRNA, and the specific amino acid. To my knowledge it is more like the enzyme is specialized for the amino acid like a lock and key situation. Here is a website that goes into more detail as well! :) https://www.nature.com/scitable/topicpage/translation-dna-to-mrna-to-protein-393/
For your third question I am not confident enough to answer that question directly however the mRNA strands do know which types of ribosomes to go to depending on where the protein needs to go after so I don’t believe proteins would have the opportunity to be where they aren’t supposed to be unless things have somehow gone very awry. From what I have read proteins with specific destinations are labeled and ones that are not remain in the cytoplasm but I don’t believe that yeilds any negative consequences. Here is an article that goes into more detail, I hope that helps! http://oregonstate.edu/instruction/bi314/summer09/trafficking.html
To answer your first question, after researching there has been no mention of a different process capable of synthesizing protein from mRNA. It is common to see translation referred to as protein synthesis instead of translation though. Hope this helps!
1 - How does the tRNA strand and the enzyme find the appropriate amino acid? 2 - What happens if an error occurs during translation? Will it terminate the sequence? 3 - How fast does the release factor work once the stop codon triggers it?
In response to your second question, it is possible for the sequence to be terminated and the protein not be made, but often something else happens because of a translation error. Another possibility that could stem from a translation error would be mutations in the protein instead of it just not being created, which has the ability to greatly impact the organism the protein was created for as a whole. In the case of gamete translation errors, the offspring could have negative effects born as a result. My sources are listed below, I hope this helps!
In response to your third question, the release factor works fairly quickly after receiving the signal from the stop codon. Of course the reaction time with change and shift a bit, but overall if the stop codon is coded correctly and is read correctly it should stop pretty quickly. I had a hard time finding good sources for this one, but I hope the included one helps a bit! It has more details about stop codon recognition.
1. Why are amino acids important to the process of translation, and what would happen if there were a shortage of them in the process? 2. How can you tell the difference between the 3' side and the '5 side during translation? 3. How do amino acids get to the ribosome in the first place during translation?
3- the amino acids are attached to the tRNA. The tRNA then enters the ribosome and attaches to the mRNA in the A site. The t in tRNA stands for transport and their job is to transfer amino acids to make the polypeptide.
To answer your first question, amino acids are important because they are responsible for body protein and compounds containing nitrogen synthesis. If there is a shortage or an amino acid is missing, protein synthesis will stop and the chain will be broken down into individual amino acids or it will be taken in by the liver. https://www.ncbi.nlm.nih.gov/books/NBK234922/
3: Most amino acids can be found in the cytoplasm making them "free floating". If you'd like more information on how amino acids come into the body check ths source out- https://bscb.org/learning-resources/softcell-e-learning/ribosome/#:~:text=Provision%3A%20Amino%20acids%2C%20mainly%20supplied,synthesis%20site%20in%20the%20ribosome.
1. Is it possible for the ribosomes to mistake the start codon AUG for another part of the mRNA strand? what would happen? 2. What exactly is the release factor? How is the release factor produced? 3. Can modifications to the translated polypeptide happen after the translation period?
3- I found some really cool information about this! The answer is yes. There is this thing called PTM or Posttranslational Modification.It can happen at any point after translation. This is a super short, clear, and interesting couple paragraphs all about it: https://www.sciencedirect.com/topics/biochemistry-genetics-and-molecular-biology/posttranslational-modification
Question 2- The release factor is a protein which is able to recognize when to terminate the process of translation. Perhaps this link would be able to help your understanding :)
1. What would happen if a mistake occurred during translation 2. Is there a defect, disease, or external factor that can cause failure in the translation process? 3. What would happen to a cell with a faulty ribosome?
Question 1- I would imagine that if there were a mistake during translation, the body would be able to recognize it and stop it before any damage can be done. Similar to how the body knows when a cell is defective and so the cell goes through the process of apoptosis.
Question 2- I couldn't find any examples of any specific diseases, however I did find an article that confirms that translation can be affected by certain diseases/disorders. Essentially, translation is not able to occur properly which greatly disrupts the body's ability to function.
1) What would happen if during the elongation phase, the correct anticodon did not bind to the codon in the 'A' site? 2) How does translation work in bacteria? 3) How do start codons work?
1. Where can errors in the process of translation occur?
ReplyDelete2. Is there an upper and lower limit to the size of the proteins formed?
3. What is AMP and what does it do?
To answer your third question, AMP is a form of ATP with only a single phosphate (adenosine mono phosphate). It is the nucleotide for adenine and also is used to be combined with natural phosphate to create ADP and then ATP.
DeleteFor your second question, there is not a biological limit, but the smallest protein found was extracted from Gila monsters and consists of 20 amino acids. The largest found is titan which consists of 27000 amino acids.
DeleteTo answer your third question, I found that AMP is adenosine monophosphate. This is very important for molecules that participate in energy processes in a living cell. Here is a website that explains this further: https://www.britannica.com/science/adenosine-monophosphate
DeleteTo answer your first question, when eukaryotic cells are exposed to E. coli, mis-translation can occur. An example of this is arginine to lysine substitution, where the arginine rare codon AGA is erroneously recognized by the tRNA that codes for lysine (UUU).
DeleteMore information can be found here: https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5491249/
It is also possible for ribosomes to read through stop codons or have premature termination.
More information about this can be found here: https://www.cell.com/trends/genetics/pdf/S0168-9525(17)30227-5.pdf
To help answer your 1st question, here is an article that goes over mistakes in translation:
Deletehttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC5491249/
1. What techniques and technology is used to predict the folding patterns of protein?
ReplyDelete2. What are evolutionary precursors to ribasomes?
3. What is a theory for how Ribosomes evolved?
For your first question the most common methods used to prdict proteins structure is x-ray crystallography and nuclear magnetic resonance. More on this can be found here: https://www.sciencedirect.com/topics/biochemistry-genetics-and-molecular-biology/protein-structure-prediction#:~:text=Currently%2C%20the%20main%20techniques%20used,structure%20of%20protein%20is%20determined.
DeleteTo answer your second question, I could not find a specific name for a precursor, however, what I found was that all ribosomes share the same base components and it is believed that this commonality is what ribosomes originally were.
Deletehttps://astrobiology.nasa.gov/news/the-ribosome-a-record-of-evolution/
In response to your third question, this site goes into great detail on how ribosomes evolved throughout the years. I'd give a description, but I am lazy.
Deletehttps://www.pnas.org/content/112/50/15396
To help answer your 2nd question, here is a website that might help:
Deletehttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC2107574/
1. How does the structure of proteins change between tertiary and quaternary structure?
ReplyDelete2. How do proteins find their way to the location that they are meant to function in?
How long does it take for proteins to get to their final form after translation?
Pretend there's a "3." before the last one
DeleteTo answer your second question, There is a tag added onto them by the golgi apparatus which tells the protein where to go.
DeleteTo answer your first question, the difference between the tertiary and quaternary structures are that the quaternary structure is multiple polypeptides whereas the tertiary structure is one polypeptide.
DeleteIn response to your third question, the amount of time it takes for a protein to fold difficult to determine. Often times it will take place in the span of a second, however, the Levinthal Paradox is a result of protein folding. The paradox is that there are many non-native configurations that are unnecessary in the protein folding that would slow the process down for an unknowable period of time. So, there is no specific measurement of the amount of time it takes a protein to fold after translation.
Deletehttps://people.chem.umass.edu/rmweis/Chem728/lectures/L09_ProFold.pdf
1. Is the space inside a ribosome open or are there compartments/dividers between the 3 binding sites?
ReplyDelete2. What is the use of AMP that is released from the enzyme that attaches the amino acid to tRNA?
3. Does the tRNA need to interact with the tRNA-activating enzyme for the 3 stop codons?
For your first question, although some of the diagrams we've used make it appear as if there were clear divides between the binding sites, this is usually to show a simplified version which is easy to understand. The process of translocation makes it impossible for there to be compartments here. The part of the amino acids facing away from the ribosome are first pulled to their new site, creating diagonal location, then the bottoms are transferred. The two amino acids which are transferred remain attached to each other, so they can't move trough compartments without a more advanced process. https://www.pnas.org/content/104/50/19671
DeleteTo answer your second question, AMP is simply the biproduct of releasing the phosphate from the ADP used by the enzyme. It's main use is to recombine with another phosphate to form ADP and then ATP.
DeleteTo answer your third question, because there is no tRNA that codes for a stop codon, when the ribosome reaches the stop codon, there is no tRNA that needs to be activated by the tRNA-activating enzyme.
DeleteSource: https://www.nature.com/scitable/definition/translation-rna-translation-173/
1. what happens in Eukaryotic cells after translation?
ReplyDelete2. Why does translation take place in the cytoplasm?
3. How long does it take for elongation to occur?
In response to your third question, the amount of time it takes for elongation depends on the length of the mRNA being translated. However, it is also known that 20 amino acids can be added per second or 60 nucleotides translated per second. So, assuming you know the length of the mRNA being translated or the polypeptide, you can determine about how long it will take for elongation to occur.
Deletehttp://book.bionumbers.org/what-is-faster-transcription-or-translation/
To answer your first question, once translation is complete, the completed polypeptides go on to their specific locations and continue to undergo modifications in order to fulfill their shapes and functions as proteins. Signal sequences are the amino acid sequences that direct the polypeptide to its ultimate destination in the body (with the help of other cellular factors). This sequence is then cut off when the protein reaches its location. Proteins destined for the cytoplasm, mitochondria, or chloroplast in plants stay within the cell. Proteins bound for outside the cell are synthesized on ribosomes on the ER and are prepared for secretion at the end of translation. The proteins then start folding into the best structure for their specific function. Sometimes molecules called chaperones are required to prevent error. I hope that this answers at least part of your question!
Deletehttps://courses.lumenlearning.com/suny-wmopen-biology1/chapter/translation/
To answer your second question, it occurs inside of the cytoplasm due to the fact that ribosomes are found in the cytoplasm.
DeleteIn response to your 3rd question, the time taken for elongation to take place can vary, but does officially end once the Stop codon is read
Delete1) Does a polypeptide’s attachment change from tRNA molecule to tRNA molecule (since one is always leaving from the E site and the polypeptide can't leave the ribosome until the stop codon is reached)? If so, how does this transfer occur?
ReplyDelete2) I am a bit confused on how tRNA activating enzymes work. Does this process of attaching an amino acid to the tRNA happen inside the ribosome (while the anticodon is paired with the mRNA codon), or happen outside of the cell first and then the tRNA with the amino acid attaches to the codon via its anticodon?
3) The textbook says that the signal sequence is the first part of the polypeptide translated. Does this mean that the signal sequence occurs before the start codon, or that it is the first codon following?
In response to your second question, the tRNA-activating enzymes are in the cytoplasm and each one has a specific amino acid that binds to it. The enzymes will find tRNA and then bind the amino acid to the tRNA . Once this has been done, the bonded tRNA is released into the cell to attach to ribosomes and participate in the translation process.
Deletehttps://ib.bioninja.com.au/higher-level/topic-7-nucleic-acids/73-translation/trna-activation.html
To answer your first question, yes the amino acid does go from tRNA to tRNA when in the ribosome. This happens between the tRNA in the E and A site. A peptide bond is formed between the amino acids and the amino acid breaks off from the P site tRNA. The tRNA then move down and the polypeptide chain is now in the same place as before. This goes on until the process is done.
DeleteTo answer your third question, as the process of translation requires the start codon to come first, the signal sequence would be the sequence following the start codon, being the first to be translated after translation begins.
Delete1) Why does a tRNA molecule have to be recharged?
ReplyDelete2) Anyone have a mnemonic for remembering the processes of transcription and translation?
3) Are there more types of RNA?
For your third question I found that there are many types of RNA, but the three most well known are mRNA (messenger RNA),tRNA (transfer RNA) and rRNA (ribosomal RNA).There is also small nuclear rna (snRNA), regulatory RNAs, double-stranded RNAs (dsRNA) and many more other types that are used in all different types of cells! Hope this helped :)
DeleteTo answer your first question, I found this exact situation on bioninja :)
Delete"The function of the ATP phosphorylation is to create a high energy bond that is transferred to the tRNA molecule. This stored energy will provide the majority of the energy required for peptide bond formation during translation."
https://ib.bioninja.com.au/higher-level/topic-7-nucleic-acids/73-translation/trna-activation.html
The ATP helps to form the amino acid-AMP complex, attach the corresponding amino acid to the tRNA, and leave the tRNA molecule with high enough energy for peptide connection between amino acids in the ribosome. It needs to be charged with this energy each time it helps to build a polypeptide in translation. I hope that this helps!
To answer your second question I have one that outlays the general process but its pretty wacky. It’s “Sometimes My Tarantula Exaggerates Lots Except on Tuesdays”.
DeleteS - SUBUNIT ribosome
M - MRNA binds
T - TRNA
E - ENERGY is used
L - LG SUBUNIT is added
E - ELONGATION
T - TERMINATION
I don’t have a source from this but here is an interesting read on the general process.
https://www.khanacademy.org/science/biology/gene-expression-central-dogma/translation-polypeptides/a/the-stages-of-translation
For your second question I found that in translation the amino acids stop elongating, or getting added onto, when the stop codon is read my the tRNA. TRNA cannot code the stop codon of the mRNA, the three stop codons being, UAA, UGA or UAG, because there is no anticodon that can be complementary paired with them. In conclusion, the whole process of translation, including the elongation of amino acids, is stopped when the stop codon is translated.
ReplyDeleteTo answer your third question, translation does occur in the same place in both prokaryotes and eukaryotes: the cytoplasm (more specifically in the cytosol in prokaryotes). The difference in translation between the two is that it occurs simultaneously with transcription in prokaryotes, and discontinuously in eukaryotes. This is because eukaryotes are compartmentalized and keep the DNA within the nucleus. It must make post-transcriptional modifications before the MRNA can exit the nucleus, which results in a slower process than prokaryotic cells. Also, the mRNA will in prokaryotes will not be utilizing ribosomes located on the rough ER, as there is none in a prokaryotic cell. I hope that this helps!
ReplyDelete1. How are amino acids constructed?
ReplyDelete2. Do ribosomes have an exact partner in terms of small to large, or are they independent pieces that can join together with any other piece?
3. What causes the large half of the ribosome to hook on to the smaller half only when mRNA and tRNA are present?
For your third question, the amino acids hooking onto the enzymes are represented by a three-nucleotide sequence or codon along the mRNA molecule. This specializes the amino acids and other molecules with mRNA. For more information, the source that helped me was https://www.nature.com/scitable/topicpage/ribosomes-transcription-and-translation-14120660/#:~:text=Ribosomes%20are%20the%20sites%20in,which%20protein%20synthesis%20takes%20place.&text=Within%20the%20ribosome%2C%20the%20rRNA,RNA%20to%20reflect%20this%20function.
Delete1. How does mRNA know which ribosome to go to?
ReplyDelete2. How does an amino acid know which tRNA and activating enzyme is the correct one?
3. Are there instances where a tRNA molecule is malformed? If so, what happens to it?
For your third question, tRNA molecules can be mutated. If this should happen, diseases that are subject in the brain and neurological disorders will be caused. I cannot explain it as in depth, but here is the source I used for this answer, https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6716996/.
DeleteFor your second question, an amino acid is coded to where it goes to the activating enzyme. It corresponds with the tRNA. For more information, the source I used was https://www.nature.com/scitable/topicpage/ribosomes-transcription-and-translation-14120660/#:~:text=Ribosomes%20are%20the%20sites%20in,which%20protein%20synthesis%20takes%20place.&text=Within%20the%20ribosome%2C%20the%20rRNA,RNA%20to%20reflect%20this%20function.
Delete1. How are the amino acids specialized for the enzyme?
ReplyDelete2. Do cells ever create useless proteins?
3. After the proteins are secreted, can they end up in a place where they are not supposed to be? How would this effect the cell if so?
In response to your second question; there are proteins that are thought to be pretty much useless, but they actually perform small tasks that aren't studied as often, such as varying structural purposes. Even the spare DNA bits that get taken off and left behind after the transcription process that never get made into proteins can have uses that are being discovered, such as amplifying gene expression and the development of mutations such as breast cancer and autism. SO in short, I do not believe that there are any proteins or DNA strands that are completely useless. I hope this helps!
DeleteSource :)
https://www.discovermagazine.com/health/our-cells-are-filled-with-junk-dna-heres-why-we-need-it
To answer your first question, the enzymes have special bonding sites for the energy source, tRNA, and the specific amino acid. To my knowledge it is more like the enzyme is specialized for the amino acid like a lock and key situation. Here is a website that goes into more detail as well! :)
Deletehttps://www.nature.com/scitable/topicpage/translation-dna-to-mrna-to-protein-393/
For your third question I am not confident enough to answer that question directly however the mRNA strands do know which types of ribosomes to go to depending on where the protein needs to go after so I don’t believe proteins would have the opportunity to be where they aren’t supposed to be unless things have somehow gone very awry. From what I have read proteins with specific destinations are labeled and ones that are not remain in the cytoplasm but I don’t believe that yeilds any negative consequences. Here is an article that goes into more detail, I hope that helps! http://oregonstate.edu/instruction/bi314/summer09/trafficking.html
DeleteTo answer your first question, after researching there has been no mention of a different process capable of synthesizing protein from mRNA. It is common to see translation referred to as protein synthesis instead of translation though. Hope this helps!
ReplyDelete1 - How does the tRNA strand and the enzyme find the appropriate amino acid?
ReplyDelete2 - What happens if an error occurs during translation? Will it terminate the sequence?
3 - How fast does the release factor work once the stop codon triggers it?
In response to your second question, it is possible for the sequence to be terminated and the protein not be made, but often something else happens because of a translation error. Another possibility that could stem from a translation error would be mutations in the protein instead of it just not being created, which has the ability to greatly impact the organism the protein was created for as a whole. In the case of gamete translation errors, the offspring could have negative effects born as a result. My sources are listed below, I hope this helps!
DeleteSources :)
https://www.pnas.org/content/113/12/3311#:~:text=However%2C%20errors%20that%20occur%20during,producing%20misfolded%20and%20malfunctioning%20proteins.&text=Therefore%2C%20a%20single%20transcription%20error,disrupt%20only%20a%20single%20protein.
https://www.chapelhillisd.org/cms/lib6/TX01917727/Centricity/Domain/518/Mutations%20that%20happen%20during%20Transcription%20and%20Translation.pptx
In response to your third question, the release factor works fairly quickly after receiving the signal from the stop codon. Of course the reaction time with change and shift a bit, but overall if the stop codon is coded correctly and is read correctly it should stop pretty quickly. I had a hard time finding good sources for this one, but I hope the included one helps a bit! It has more details about stop codon recognition.
DeleteSource :)
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2789991/
1. Why are amino acids important to the process of translation, and what would happen if there were a shortage of them in the process?
ReplyDelete2. How can you tell the difference between the 3' side and the '5 side during translation?
3. How do amino acids get to the ribosome in the first place during translation?
2- The 3 prime side always ends with CCA! The 3 prime end is where the amino acid attaches as well. It attaches through an Ester bond :)
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Delete3- the amino acids are attached to the tRNA. The tRNA then enters the ribosome and attaches to the mRNA in the A site. The t in tRNA stands for transport and their job is to transfer amino acids to make the polypeptide.
DeleteTo answer your first question, amino acids are important because they are responsible for body protein and compounds containing nitrogen synthesis. If there is a shortage or an amino acid is missing, protein synthesis will stop and the chain will be broken down into individual amino acids or it will be taken in by the liver.
Deletehttps://www.ncbi.nlm.nih.gov/books/NBK234922/
1. What is the energy that GTP->GDP produces used for?
ReplyDelete2. How are tRNA and the amino acid attached?
3. Are amino acids free floating?
2: The 3'end of tRNA attaches to the amino acid through an aminoacyl bond. https://www.oxfordreference.com/view/10.1093/oi/authority.20110810104341635
Delete3: Most amino acids can be found in the cytoplasm making them "free floating". If you'd like more information on how amino acids come into the body check ths source out-
Deletehttps://bscb.org/learning-resources/softcell-e-learning/ribosome/#:~:text=Provision%3A%20Amino%20acids%2C%20mainly%20supplied,synthesis%20site%20in%20the%20ribosome.
1. Is it possible for the ribosomes to mistake the start codon AUG for another part of the mRNA strand? what would happen?
ReplyDelete2. What exactly is the release factor? How is the release factor produced?
3. Can modifications to the translated polypeptide happen after the translation period?
3- I found some really cool information about this! The answer is yes. There is this thing called PTM or Posttranslational Modification.It can happen at any point after translation. This is a super short, clear, and interesting couple paragraphs all about it: https://www.sciencedirect.com/topics/biochemistry-genetics-and-molecular-biology/posttranslational-modification
DeleteQuestion 2- The release factor is a protein which is able to recognize when to terminate the process of translation. Perhaps this link would be able to help your understanding :)
Deletehttps://link.springer.com/article/10.1007/BF00986959
1. What would happen if a mistake occurred during translation
ReplyDelete2. Is there a defect, disease, or external factor that can cause failure in the translation process?
3. What would happen to a cell with a faulty ribosome?
Question 1- I would imagine that if there were a mistake during translation, the body would be able to recognize it and stop it before any damage can be done. Similar to how the body knows when a cell is defective and so the cell goes through the process of apoptosis.
DeleteQuestion 2- I couldn't find any examples of any specific diseases, however I did find an article that confirms that translation can be affected by certain diseases/disorders. Essentially, translation is not able to occur properly which greatly disrupts the body's ability to function.
Deletehttps://www.nature.com/scitable/content/translation-matters-protein-synthesis-defects-in-inherited-13998175/
1) What would happen if during the elongation phase, the correct anticodon did not bind to the codon in the 'A' site?
ReplyDelete2) How does translation work in bacteria?
3) How do start codons work?