Exam 10: Protein Synthesis, Processing, and Regulation

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The first amino acid that initiates the eukaryotic polypeptide is

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To function as a repressor-binding site, the iron response element (IRE) must be within the first 70 nucleotides of the ferritin mRNA. This suggests that protein binding to this IRE

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Prior to N-linked glycosylation of a protein, a complex oligosaccharide is assembled in the endoplasmic reticulum on a lipid carrier called

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Which statement about translational regulation of ferritin is false?

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Peptide bond formation in translation occurs by

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Aminoacyl tRNA synthetases are enzymes that

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The primary function of rRNAs in the ribosome is to

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Cells contain 64 tRNAs, with one anticodon for each codon.

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In cystic fibrosis patients, deletion of an amino acid (phenylalanine 508) in the CFTR protein

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The adapters that align amino acids in a sequence determined by the mRNAs are called _______.

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Translation starts at a particular start codon near the _______ end of the mRNA.

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A complex of eukaryotic initiation factors (eIF4E, eIF4G, eIF4A, and eIF4B) brings the mRNA to the 40S ribosomal subunit and is thought to unwind base-paired structures in the mRNA to allow for the codon‒anticodon interactions necessary for translation of the message. What is the most likely reason that an equivalent activity is not present in prokaryotic cells?

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Protein synthesis occurs on RNA-protein complexes called _______.

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One molecule of GTP is split in the process of loading one amino acid onto its tRNA.

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The combined sizes of prokaryotic and eukaryotic ribosomes are

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Nitrosylation occurs on the side chain of

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Suppose that a single protein is significantly overexpressed in one of two different cell lines. The proteins are identical, but Northern blot analysis indicates that the mRNA for the protein in the overexpressing cell line is about 200 base pairs shorter. Subsequent reverse transcriptase PCR has revealed that the truncation occurs in the 3ʹ untranslated region. How might this lead to overexpression of the protein?

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The proteins shaped like a "double chamber" that are involved in protein folding are called

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