Getting Access to Low-Complexity Domain Modifications

Roland Schüller; Dirk Eick

doi:10.1016/j.tibs.2016.05.010

Getting Access to Low-Complexity Domain Modifications

Trends Biochem Sci. 2016 Nov;41(11):894-897. doi: 10.1016/j.tibs.2016.05.010. Epub 2016 Jun 6.

Authors

Roland Schüller¹, Dirk Eick²

Affiliations

¹ Department of Molecular Epigenetics, Helmholtz Center Munich and Center for Integrated Protein Science Munich (CIPSM), Marchioninistrasse 25, 81377 Munich, Germany.
² Department of Molecular Epigenetics, Helmholtz Center Munich and Center for Integrated Protein Science Munich (CIPSM), Marchioninistrasse 25, 81377 Munich, Germany. Electronic address: eick@helmholtz-muenchen.de.

PMID: 27283512
DOI: 10.1016/j.tibs.2016.05.010

Abstract

Low-complexity (LC) domains regulate the aggregation and phase transition of proteins in a modification-dependent manner. The study of LC domain modifications has now become feasible, as shown by genetic variants of the carboxy-terminal domain (CTD) of RNA Polymerase II (Pol II) that provide access to the type and position of modifications of a LC domain by mass spectrometry (MS).

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Amino Acid Sequence
Amino Acid Substitution*
Animals
Calmodulin-Binding Proteins / chemistry*
Calmodulin-Binding Proteins / genetics
Chickens
Gene Expression
Humans
Mice
Mutation
Protein Domains
RNA Polymerase II / chemistry*
RNA Polymerase II / genetics
RNA-Binding Protein EWS
RNA-Binding Protein FUS / chemistry*
RNA-Binding Protein FUS / genetics
RNA-Binding Proteins / chemistry*
RNA-Binding Proteins / genetics
Sequence Alignment
Sequence Homology, Amino Acid
TATA-Binding Protein Associated Factors / chemistry*
TATA-Binding Protein Associated Factors / genetics
Transcription, Genetic

Substances

Calmodulin-Binding Proteins
EWSR1 protein, human
FUS protein, human
RNA-Binding Protein EWS
RNA-Binding Protein FUS
RNA-Binding Proteins
TAF15 protein, human
TATA-Binding Protein Associated Factors
RNA Polymerase II