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Ch. 18 - Post-transcriptional Regulation in Eukaryotes
Klug - Concepts of Genetics  12th Edition
Klug12th EditionConcepts of Genetics ISBN: 9780135564776당신이 사용하는 게 아니라요?교과서 변경
18장, 문제 21

How may the covalent modification of a protein with a phosphate group alter its function?

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1
Understand that covalent modification refers to the addition or removal of a chemical group to a protein, which can change the protein's properties and activity.
Recognize that phosphorylation is the addition of a phosphate group (PO₄³⁻) to specific amino acid residues, commonly serine, threonine, or tyrosine, in the protein.
Consider how the addition of a negatively charged phosphate group can induce a conformational change in the protein's three-dimensional structure, potentially altering its shape and function.
Analyze how this conformational change can affect the protein's activity by either activating or inhibiting its enzymatic function, altering its interaction with other molecules, or changing its cellular localization.
Summarize that phosphorylation acts as a regulatory mechanism, allowing cells to control protein function dynamically in response to various signals.

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Protein Phosphorylation

Protein phosphorylation is the covalent addition of a phosphate group, usually to serine, threonine, or tyrosine residues. This modification is catalyzed by enzymes called kinases and can change the protein's activity, interactions, or localization.
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Conformational Change

The addition of a phosphate group can induce a conformational change in the protein's structure. This structural alteration can activate or inhibit the protein's function by exposing or hiding active sites or interaction domains.
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Regulation of Protein Function

Phosphorylation acts as a regulatory mechanism, controlling processes like enzyme activity, signal transduction, and protein-protein interactions. It is reversible, allowing dynamic control through phosphatases that remove phosphate groups.
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Incorrectly spliced RNAs often lead to human pathologies. Scientists have examined cancer cells for splice-specific changes and found that many of the changes disrupt tumor-suppressor gene function [Xu and Lee (2003). Nucl. Acids Res. 31:5635–5643]. In general, what would be the effects of splicing changes on these RNAs and the function of tumor-suppressor gene function? How might loss of splicing specificity be associated with cancer?

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What role do ubiquitin ligases play in the regulation of gene expression?

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How and why are eukaryotic mRNAs transported and localized to discrete regions of the cell?

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