How does an anticodon participate in protein synthesis

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Subject optional. Email address: Your name:. Possible Answers: DNA. Correct answer: tRNA. Explanation : Each tRNA contains the anticodon for a specific mRNA codon and carries the amino acid corresponding to that codon to ribosomes during translation.

Report an Error. Possible Answers: tRNA. What is its corresponding tRNA anticodon? Possible Answers: 3'-TTG-5'. Correct answer: 3'-UUG-5'. Explanation : An anticodon is the three-base sequence, paired with a specific amino acid, that a tRNA molecule brings to the corresponding codon of the mRNA during translation. Possible Answers: rRNA. Explanation : Anticodons are found on molecules of tRNA.

Possible Answers: To aid in the transcription of genes. To bring information from within the nucleus to the cytoplasm. Correct answer: To bring amino acids to ribosomes. Explanation : tRNA is a special type of RNA that has the function of forming bonds with amino acids and bringing them to ribosomes to complete translation.

How does a ribosome detect that the correct amino acid is being added during translation? Explanation : Amino acid sequence is determined by the sequence of codons on mRNA. Possible Answers: Translation. Correct answer: Translation. Which of the following correctly pairs each kind of RNA with its function? Which of the following choices is the enzyme that adds amino acids to tRNA molecules?

Possible Answers: Primase. Correct answer: Aminoacyl-tRNA synthetase. How are ribosomal units typically organized during translation? Possible Answers: Two small subunits. Correct answer: A large subunit and a small subunit.

Explanation : Ribosomes are non-membranous organelles that direct protein synthesis by reading mRNA and joining amino acids into strands of polypeptides. Copyright Notice. View AP Biology Tutors. Margely Certified Tutor. Lalita Certified Tutor. Meghana Certified Tutor. Report an issue with this question If you've found an issue with this question, please let us know.

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I have a good faith belief that the use of the material in the manner complained of is not authorized by the copyright owner, its agent, or the law. This notification is accurate.

I acknowledge that there may be adverse legal consequences for making false or bad faith allegations of copyright infringement by using this process. The large subunit of the ribosome has three sites at which tRNA molecules can bind.

The A amino acid site is the location at which the aminoacyl-tRNA anticodon base pairs up with the mRNA codon, ensuring that correct amino acid is added to the growing polypeptide chain.

The P polypeptide site is the location at which the amino acid is transferred from its tRNA to the growing polypeptide chain. Finally, the E exit site is the location at which the "empty" tRNA sits before being released back into the cytoplasm to bind another amino acid and repeat the process.

The ribosome is thus ready to bind the second aminoacyl-tRNA at the A site, which will be joined to the initiator methionine by the first peptide bond Figure 5.

Figure 5: The large ribosomal subunit binds to the small ribosomal subunit to complete the initiation complex. The initiator tRNA molecule, carrying the methionine amino acid that will serve as the first amino acid of the polypeptide chain, is bound to the P site on the ribosome. The A site is aligned with the next codon, which will be bound by the anticodon of the next incoming tRNA.

Next, peptide bonds between the now-adjacent first and second amino acids are formed through a peptidyl transferase activity. For many years, it was thought that an enzyme catalyzed this step, but recent evidence indicates that the transferase activity is a catalytic function of rRNA Pierce, After the peptide bond is formed, the ribosome shifts, or translocates, again, thus causing the tRNA to occupy the E site.

The tRNA is then released to the cytoplasm to pick up another amino acid. In addition, the A site is now empty and ready to receive the tRNA for the next codon. This process is repeated until all the codons in the mRNA have been read by tRNA molecules, and the amino acids attached to the tRNAs have been linked together in the growing polypeptide chain in the appropriate order. At this point, translation must be terminated, and the nascent protein must be released from the mRNA and ribosome.

No tRNAs recognize these codons. Thus, in the place of these tRNAs, one of several proteins, called release factors, binds and facilitates release of the mRNA from the ribosome and subsequent dissociation of the ribosome.

The translation process is very similar in prokaryotes and eukaryotes. Although different elongation, initiation, and termination factors are used, the genetic code is generally identical.

As previously noted, in bacteria, transcription and translation take place simultaneously, and mRNAs are relatively short-lived. In eukaryotes, however, mRNAs have highly variable half-lives, are subject to modifications, and must exit the nucleus to be translated; these multiple steps offer additional opportunities to regulate levels of protein production, and thereby fine-tune gene expression.

Chapeville, F. On the role of soluble ribonucleic acid in coding for amino acids. Proceedings of the National Academy of Sciences 48 , — Crick, F.

On protein synthesis. Symposia of the Society for Experimental Biology 12 , — Flinta, C. Sequence determinants of N-terminal protein processing. European Journal of Biochemistry , — Grunberger, D. Codon recognition by enzymatically mischarged valine transfer ribonucleic acid. Science , — doi Kozak, M. Point mutations close to the AUG initiator codon affect the efficiency of translation of rat preproinsulin in vivo.

Nature , — doi Point mutations define a sequence flanking the AUG initiator codon that modulates translation by eukaryotic ribosomes. Cell 44 , — An analysis of 5'-noncoding sequences from vertebrate messenger RNAs.

Nucleic Acids Research 15 , — Shine, J. Determinant of cistron specificity in bacterial ribosomes. Nature , 34—38 doi Restriction Enzymes. Genetic Mutation. Functions and Utility of Alu Jumping Genes. Transposons: The Jumping Genes. DNA Transcription. What is a Gene? Colinearity and Transcription Units. Copy Number Variation. Copy Number Variation and Genetic Disease. Copy Number Variation and Human Disease.

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The process of translation can be seen as the decoding of instructions for making proteins, involving mRNA in transcription as well as tRNA. Aa Aa Aa. Figure Detail. Where Translation Occurs. Figure 3: A DNA transcription unit.

A DNA transcription unit is composed, from its 3' to 5' end, of an RNA-coding region pink rectangle flanked by a promoter region green rectangle and a terminator region black rectangle. Genetics: A Conceptual Approach , 2nd ed.

All rights reserved. The Elongation Phase. Figure 6. Termination of Translation. Comparing Eukaryotic and Prokaryotic Translation. References and Recommended Reading Chapeville, F.

European Journal of Biochemistry , — Grunberger, D. Nucleic Acids Research 15 , — Pierce, B. Article History Close.

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