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Ch. 21 - Genomic Analysis
Chapter 20, Problem 19

Annotation of the human genome sequence reveals a discrepancy between the number of protein-coding genes and the number of predicted proteins actually expressed by the genome. Proteomic analysis indicates that human cells are capable of synthesizing more than 100,000 different proteins and perhaps three times this number. What is the discrepancy, and how can it be reconciled?

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1
Understand that the human genome contains approximately 20,000 to 25,000 protein-coding genes, which is significantly less than the number of proteins expressed.
Recognize that alternative splicing is a key mechanism that allows a single gene to produce multiple protein isoforms by rearranging exons in different combinations.
Consider the role of post-translational modifications, such as phosphorylation, glycosylation, and ubiquitination, which can alter protein function and increase diversity.
Acknowledge the impact of gene regulation and expression levels, where different tissues or conditions can lead to the production of different proteins from the same gene.
Explore the concept of protein complexes and interactions, where proteins can combine in various ways to form new functional units, further increasing the diversity of the proteome.

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Key Concepts

Here are the essential concepts you must grasp in order to answer the question correctly.

Gene Expression and Alternative Splicing

Gene expression refers to the process by which information from a gene is used to synthesize functional gene products, typically proteins. Alternative splicing is a mechanism that allows a single gene to produce multiple protein isoforms by including or excluding certain sequences during RNA processing. This can lead to a situation where fewer protein-coding genes can generate a much larger variety of proteins, contributing to the observed discrepancy.
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Post-Translational Modifications

Post-translational modifications (PTMs) are chemical changes that occur to proteins after their synthesis, which can significantly alter their function, activity, and stability. These modifications, such as phosphorylation, glycosylation, and ubiquitination, can create diverse protein forms from a single polypeptide chain, further increasing the number of functional proteins beyond the number of genes.
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Proteomics and Protein Diversity

Proteomics is the large-scale study of proteins, particularly their functions and structures. It encompasses techniques that analyze the entire protein complement of a cell or organism, revealing the complexity and diversity of proteins produced. The ability of human cells to synthesize over 100,000 different proteins highlights the intricate regulatory mechanisms and interactions that contribute to protein diversity, which can exceed the number of genes.
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