TY - JOUR
T1 - Cross-β polymerization of low complexity sequence domains
AU - Kato, Masato
AU - McKnight, Steven L.
N1 - Funding Information:
This work is supported by a grant from the National Institutes of Health (U01GM107623) and unrestricted funds provided to S.L.M. by an anonymous donor.
Publisher Copyright:
© 2017 Cold Spring Harbor Laboratory Press; all rights reserved.
PY - 2017/3
Y1 - 2017/3
N2 - Most transcription factorsand RNA regulatory proteins encoded by eukaryotic genomes ranging from yeast to humans contain polypeptide domains variously described as intrinsically disordered, prion-like, or of low complexity (LC). These LC domains exist in an unfolded state when DNA and RNA regulatory proteins are studied in biochemical isolation from cells. Upon incubation in the purified state, many of these LC domains polymerize into homogeneous, labile amyloid-like fibers. Here, we consider several lines of evidence that may favor biologic utility for LC domain polymers.
AB - Most transcription factorsand RNA regulatory proteins encoded by eukaryotic genomes ranging from yeast to humans contain polypeptide domains variously described as intrinsically disordered, prion-like, or of low complexity (LC). These LC domains exist in an unfolded state when DNA and RNA regulatory proteins are studied in biochemical isolation from cells. Upon incubation in the purified state, many of these LC domains polymerize into homogeneous, labile amyloid-like fibers. Here, we consider several lines of evidence that may favor biologic utility for LC domain polymers.
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U2 - 10.1101/cshperspect.a023598
DO - 10.1101/cshperspect.a023598
M3 - Article
C2 - 27836835
AN - SCOPUS:85014627153
SN - 1943-0264
VL - 9
JO - Cold Spring Harbor Perspectives in Biology
JF - Cold Spring Harbor Perspectives in Biology
IS - 3
M1 - a023598
ER -