The number of protein-encoding genes in a prokaryotic cell equals the number of proteins that can be expressed in the same cell. However, a eukaryotic cell can express many more proteins than the number of protein-encoding genes in the same cell. Why is this the case? Explain in one sentence only.

The number of protein-encoding genes in a prokaryotic cell equals the number of proteins that can be expressed in the same cell. However, a eukaryotic cell can express many more proteins than the number of protein-encoding genes in the same cell. Why is this the case? Explain in one sentence only.

Name: The number of protein-encoding genes in a prokaryotic cell equals the
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Description: The number of protein-encoding genes in a prokaryotic cell equals the number of proteins that can be expressed inthe same cell. However, a eukaryotic cell can express many more proteins than the number of protein-encodinggenes in the same cell. Why

Biology 2e

2nd Edition

ISBN:9781947172517

Author:Matthew Douglas, Jung Choi, Mary Ann Clark

Publisher:Matthew Douglas, Jung Choi, Mary Ann Clark

Chapter16: Gene Expression

Section: Chapter Questions

Problem 18RQ: IS. Alternative splicing has been estimated to occur in more than 95% of multi-exon genes. Which of...

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IS. Alternative splicing has been estimated to occur in more than 95% of multi-exon genes. Which of the following is not an evolutionary advantage of alternative splicing? Alternative splicing increases diversity without increasing genome size Different gene isoforms can be expressed in different tissues Alternative splicing creates shorter mRNA transcripts Different gene isoforms can be expressed during different stages of development.
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During the process of in eukaryotic cells, a in the cytoplasm is read by a in the direction, and the outcome of this process is the synthesis of a with a directionality that matches the 5' to 3' polarity of the transcript.
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The Saccharomyces cerevisiae nuclear gene ARG8encodes an enzyme that catalyzes a key step in biosynthesis of the amino acid arginine. This protein isnormally synthesized on cytoplasmic ribosomes, butthen is transported into mitochondria, where the enzyme conducts its functions. In 1996, T. D. Fox andhis colleagues constructed a strain of yeast in which agene encoding the Arg8 protein was itself moved intomitochondria, where functional protein could besynthesized on mitochondrial ribosomes.a. How could these investigators move the ARG8gene from the nucleus into the mitochondria, whilepermitting the synthesis of active enzyme? In whatways would the investigators need to alter theARG8 gene to allow it to function in the mitochondria instead of in the nucleus?b. Why might these researchers have wished to movethe ARG8 gene into mitochondria in the firstplace?
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