TY - JOUR
T1 - A Solid-State Conceptualization of Information Transfer from Gene to Message to Protein
AU - Kato, Masato
AU - McKnight, Steven L.
N1 - Funding Information:
We thank Tina Han, Xinlin Du, Shanhai Xie, Ilmin Kwon, Siheng Xiang, Yi Lin, Xiaoming Zhou, Kevin Shi, Eiichiro Mori, Leeju Wu, Lillian Sutherland, Vasily Sysoev, Elizabeth Goldsmith, David Eisenberg, Jeff Corden, Dylan Murray, and Robert Tycko for working with us over the past six years on the science described in this review; Deepak Nijhawan, Benjamin Tu, Paul Taylor, Richard Losick, and Charles Emerson for long-standing intellectual input; Bruce Stillman, Robert Tjian, Bruce Alberts, Joan Steitz, Michael Brown, Joe Goldstein, Tom Cech, Jacob Schwartz, Arthur Horwich, Susan Strome, Geraldine Seydoux, Roy Parker, Bill Neaves, Lisa Conti, and John Gurdon for reading our manuscript prior to publication; Andrea Roth for administrative assistance; and the National Institute for General Medical Sciences and the generosity of an anonymous donor for financial support provided to the McKnight laboratory at UT Southwestern Medical Center.
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
UR - http://www.scopus.com/inward/record.url?scp=85048251447&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=85048251447&partnerID=8YFLogxK
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 -