Cross-β polymerization of low complexity sequence domains

Research output: Contribution to journalArticle

15 Citations (Scopus)

Abstract

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.

Original languageEnglish (US)
Article numbera023598
JournalCold Spring Harbor perspectives in biology
Volume9
Issue number3
DOIs
StatePublished - Mar 1 2017

Fingerprint

Polymerization
RNA
Cell Separation
Prions
Transcription
Amyloid
Yeast
Polymers
Proteins
Genes
Yeasts
Genome
Peptides
DNA

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)

Cite this

Cross-β polymerization of low complexity sequence domains. / Kato, Masato; McKnight, Steven L.

In: Cold Spring Harbor perspectives in biology, Vol. 9, No. 3, a023598, 01.03.2017.

Research output: Contribution to journalArticle

@article{92d4b32174e547ca8a6ec5ffb46b9984,
title = "Cross-β polymerization of low complexity sequence domains",
abstract = "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.",
author = "Masato Kato and McKnight, {Steven L.}",
year = "2017",
month = "3",
day = "1",
doi = "10.1101/cshperspect.a023598",
language = "English (US)",
volume = "9",
journal = "Cold Spring Harbor perspectives in biology",
issn = "1943-0264",
publisher = "Cold Spring Harbor Laboratory Press",
number = "3",

}

TY - JOUR

T1 - Cross-β polymerization of low complexity sequence domains

AU - Kato, Masato

AU - McKnight, Steven L.

PY - 2017/3/1

Y1 - 2017/3/1

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.

UR - http://www.scopus.com/inward/record.url?scp=85014627153&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=85014627153&partnerID=8YFLogxK

U2 - 10.1101/cshperspect.a023598

DO - 10.1101/cshperspect.a023598

M3 - Article

C2 - 27836835

AN - SCOPUS:85014627153

VL - 9

JO - Cold Spring Harbor perspectives in biology

JF - Cold Spring Harbor perspectives in biology

SN - 1943-0264

IS - 3

M1 - a023598

ER -