TY - JOUR
T1 - A Solid-State Conceptualization of Information Transfer from Gene to Message to Protein
AU - Kato, Masato
AU - McKnight, Steven L.
N1 - Publisher Copyright:
© 2018 by Annual Reviews. All rights reserved.
PY - 2018/6/20
Y1 - 2018/6/20
N2 - 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.
AB - 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.
KW - aliphatic alcohols
KW - hydrogels
KW - intrinsically disordered proteins
KW - labile cross-β interactions
KW - liquid-like droplets
KW - low complexity domains
KW - phase transitions
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U2 - 10.1146/annurev-biochem-061516-044700
DO - 10.1146/annurev-biochem-061516-044700
M3 - Review article
C2 - 29195049
AN - SCOPUS:85048251447
SN - 0066-4154
VL - 87
SP - 351
EP - 390
JO - Annual review of biochemistry
JF - Annual review of biochemistry
ER -