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Cross-β Polymerization of Low Complexity Sequence Domains
Author(s) -
Masato Kato,
Steven L. McKnight
Publication year - 2016
Publication title -
cold spring harbor perspectives in biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 6.011
H-Index - 173
ISSN - 1943-0264
DOI - 10.1101/cshperspect.a023598
Subject(s) - biology , rna , dna , transcription (linguistics) , homogeneous , yeast , polymerization , computational biology , microbiology and biotechnology , transcription factor , biochemistry , gene , polymer , chemistry , organic chemistry , philosophy , linguistics , physics , thermodynamics
Most transcription factors and 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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