Order the following choices to indicate the sequence of steps in the process of elongation of a growing peptide chain. Peptidyltransferase reaction catalyzed by large rRNA subunit. Aminoacyl-tRNA binds the ribosomal A site via EF1x-GTP hydrolysis. EF2-GTP hydrolysis promotes translocation of the ribosome. Release of EF1x-GDP.

Order the following choices to indicate the sequence of steps in the process of elongation of a growing peptide chain. Peptidyltransferase reaction catalyzed by large rRNA subunit. Aminoacyl-tRNA binds the ribosomal A site via EF1x-GTP hydrolysis. EF2-GTP hydrolysis promotes translocation of the ribosome. Release of EF1x-GDP.

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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The synthesis of a protein requires that the amino acids that constitute the growing polypeptide chain be covalently linked to the amino acid attached to the tRNA at the aminoacyl site of the ribosome. Which of the following catalyses this reaction? Options: the aminoacyl tRNA synthetase eEF2 eEF1-GTP a large ribosomal RNA the initiator tRNA met
Place the steps below in the correct order to accurately reflect the steps by which a secretory protein is co-translationally imported into the lumen of the endoplasmic reticulum: As the polypeptide elongates and translocates into the ER, the signal peptidase cleaves the signal peptide. The SRP binds the SRP receptor, directing the ribosome to dock on the ER membrane. Termination of translation, results in the release of the polypeptide into the ER lumen, release of the ribosome from the ER membrane, and closing of the channel. The signal recognition particle (SRP) binds to the signal sequence on a newly synthesized polypeptide and stalls translation. The channel in the ER membrane opens and the polypeptide is inserted into the ER lumen. The SRP is released. A.6-4-2-3-1-5 B.4-2-5-1-3-6 C.3-1-6-2-4-5 D.1-2-3-4-5-6 E.2-6-1-5-4-3
During the biosynthesis of ribosomes, rRNA synthesized in the (fill in) Nuclear membrane nucleolus Cytoplasm Nuclear pore complex And Ribosomal proteins are assembled together into the rirbosomal subunits which are then shipped to the cytoplasm where mature ribosomes are finally assembled. Free ribosomes are localized in the cytoplasm and synthesize cytoplasmic proteins such as [ans2]. While no protein synthesis takes place in the sER, it is an important site for the synthesis of (fill in) DNA tyrosine kinase receptors alcohol integrins tubulin proton pumps RNA phospholipids The sER plays also an important role in detoxification of different types of drugs, which is why ( fill in) Liver Bone Brain skin cells display a large sER. In addition, the sER functions as a reservoir for the storage of (fill in) Iron Iodine Calcium Sodium Ions in many type of cells
Renata enzymatically conjugates a 14C-labeled cysteine to a transfer RNA (ERNA), with a UGU anticodon. Then, she chemically modifies the cysteine group to valine. Finally, she adds the altered aminoacyl-tRNA to a protein-synthesizing system containing normal components and a messenger RNA (MRNA) with the sequence 5'-UUUUGCCAUGUUUGUGCU-3'. What is the sequence of the radiolabeled peptide Renata produces? Enter your answer using three-letter abbreviations for each residue, separated by single hyphens. You may need to reference a codon table. radiolabeled peptide sequence: Phe-Cys-His-Val-Ala-Ala Incorrect
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"Place the following prokaryotic translation events in order: translocation, binding of initiator tRNA, binding of release factor, assembly of small and large ribosomal subunits, peptide bond formation O Assembly of small and large ribosomal subunits, binding of release factor, peptide bond formation, binding of initiator tRNA, translocation Assembly of small and large ribosomal subunits, binding of initiator tRNA, peptide bond formation, translocation, binding of release factor O Assembly of small and large ribosomal subunits, binding of release factor, binding of initiator tRNA, peptide bond formation, translocation O Assembly of small and large ribosomal subunits, binding of initiator tRNA, translocation, peptide bond formation, binding of release factor
Which of the following interactions in E. coli ensures that the start codon of an mRNA is accurately positioned in a ribosome at the initiation of translation? O binding between the mRNA Shine-Dalgarno sequence and ribosomal proteins base-pairing between the mRNA Shine-Dalgarno sequence and rRNA of the small ribosomal subunit O binding between ribosomal proteins and the initiation factor that base-pairs with the start codon O base-pairing between the mRNA Shine-Dalgarno sequence and rRNA of the large ribosomal subunit
identify start/end site, which amino acid will be on the tRNA that is the first to bind to the A site of ribosome, anticodon on the tRNA in the P site of the ribosome when release factor bings to A site, and what amino acid sequence of the protein that will be formed from mRNA? Here is the mRNA sequence:5'GUUUCCCGUAUACAUGCGUGCCGGGGGCCCGUUACCAGGCCUCAUUAUUGGAUAACGGAAAAAAAAAAAAA3'
Which of the following cannot be said regarding aminoacyl tRNA synthetase? It is essential for the correct reading of codons. A single tRNA synthetase can attach different amino acids to their corresponding tRNA. It is first activated when it catalyzes a reaction between ATP and an amino acid to form an aminoacyladenylic acid (amino acyl-AMP). It is responsible for the attachment of the correct amino acid to the correct tRNA. There is a different tRNA synthetase for each amino acid that will be attached to a tRNA.
Several experiments were conducted to obtain information about how the eukaryotic ribosomerecognizes the AUG start codon. In one experiment, the gene that encodes the methionine initiatortRNA (tRNA,Met) was identified and changed. Specifically, the nucleotides that specify the anticodonon the tRNA,Met were mutated so that the anticodon in the tRNA was 5'-CCA-3'. When thismutated gene was introduced into a eukaryotic cell protein synthesis occurred, but the proteinsproduced were abnormal. Some of these proteins contained extra amino acids and others containedfewer amino acids than normal. a.) What is the normal anticodon for tRNA,Met? Show how this normal anticodon would interact with the codon for methionine in the mRNA. b.) What codon does the mutant anticodon bind? What amino acid is incorporated into the polypeptide chain? Show the interaction between the mutant anticodon and the amino acid codon and finally, What do the results described above indicate about how the ribosome…
Identify the correct recognition site for ribosomal subunit binding during translation. the 30s subunit binds to the 7-methylguanosine cap at the 3’ end of eukaryotic mRNA the 60s subunit binds to the “Shine-Dalgarno” sequence at the 5’ end of eubacterial mRNA the 40s subunit binds to the 7-methylguanosine cap at the 5’ end of eukaryotic mRNA the 70s subunit binds to the “Shine-Dalgarno” sequence at the 5’ end of eukaryotic mRNA the 50s subunit binds to the 7-methylguanosine cap at the 3’ end of eubacterial mRNA
RNA polymerase in Escherichia coli normally synthesizes all of the following molecules except: RNA primers during DNA replication messenger RNA (mRNA) transfer RNA (tRNA) ribosomal RNA (rRNA) heterogenous nuclear RNA (hnRNA)