Getting Access to Low-Complexity Domain Modifications.
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).
Department of Molecular Epigenetics, Helmholtz Center Munich and Center for Integrated Protein Science Munich (CIPSM), Marchioninistrasse 25, 81377 Munich, Germany.
Roland
R
Schüller
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.
Dirk
D
Eick
D000595:Amino Acid Sequence; D019943:Amino Acid Substitution; D000818:Animals; D002148:Calmodulin-Binding Proteins / Q000737:chemistry* / Q000235:genetics; D002645:Chickens; D015870:Gene Expression; D006801:Humans; D051379:Mice; D009154:Mutation; D000072417:Protein Domains; D012319:RNA Polymerase II / Q000737:chemistry* / Q000235:genetics; D034802:RNA-Binding Protein EWS; D034702:RNA-Binding Protein FUS / Q000737:chemistry* / Q000235:genetics; D016601:RNA-Binding Proteins / Q000737:chemistry* / Q000235:genetics; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D035381:TATA-Binding Protein Associated Factors / Q000737:chemistry* / Q000235:genetics; D014158:Transcription, Genetic
D002148:Calmodulin-Binding Proteins; C500986:EWSR1 protein, human; C000599550:FUS protein, human; D034802:RNA-Binding Protein EWS; D034702:RNA-Binding Protein FUS; D016601:RNA-Binding Proteins; C102041:TAF15 protein, human; D035381:TATA-Binding Protein Associated Factors; D012319:RNA Polymerase II