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Annu Rev Biochem. 2018 Jun 20;87:351-390. doi: 10.1146/annurev-biochem-061516-044700. Epub 2017 Dec 1.

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

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1
Department of Biochemistry, University of Texas Southwestern Medical Center, Dallas, Texas 75390-9152, USA; email: steven.mcknight@utsouthwestern.edu.

Abstract

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-β 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.

KEYWORDS:

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

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