4.6 Review Book Chapter

A Solid-State Conceptualization of Information Transfer from Gene to Message to Protein

期刊

ANNUAL REVIEW OF BIOCHEMISTRY, VOL 87
卷 87, 期 -, 页码 351-390

出版社

ANNUAL REVIEWS
DOI: 10.1146/annurev-biochem-061516-044700

关键词

low complexity domains; intrinsically disordered proteins; hydrogels; liquid-like droplets; phase transitions; labile cross-beta interactions; aliphatic alcohols

资金

  1. NIGMS NIH HHS [U01 GM107623] Funding Source: Medline
  2. NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [U01GM107623] Funding Source: NIH RePORTER

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In this review, we describe speculative ideas and early stage research concerning the flow of genetic information from the nuclear residence of genes to the disparate, cytoplasmic sites of protein synthesis. We propose that this process of information transfer is meticulously guided by transient structures formed from protein segments of low sequence complexity/intrinsic disorder. These low complexity domains are ubiquitously associated with regulatory proteins that control gene expression and RNA biogenesis, but they are also found in the central channel of nuclear pores, the nexus points of intermediate filament assembly, and the locations of action of other well-studied cellular proteins and pathways. Upon being organized into localized cellular positions via mechanisms utilizing properly folded protein domains, thereby facilitating elevated local concentration, certain low complexity domains adopt cross-beta interactions that are both structurally specific and labile to disassembly. These weakly tethered assemblies, we propose, are built to relay the passage of genetic information from one site to another within a cell, ensuring that the process is of extreme fidelity.

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