1. A ubiquitous disordered protein interaction module orchestrates transcription elongation
- Author
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Eric A. Smith, Zeger Debyser, Vaclav Veverka, Marcela Mádlíková, Milan Fábry, M. Horejsi, Seth R. Goldman, Vanda Lux, Monika Nedomova, H. Courtney Hodges, Pavel Srb, Jan De Rijck, Karen Adelman, Jonas Demeulemeester, Rozálie Hexnerová, and Katerina Cermakova
- Subjects
Models, Molecular ,Transcription Elongation, Genetic ,Transcription elongation ,Gene Expression ,RNA polymerase II ,Article ,Protein Domains ,Cell Line, Tumor ,Humans ,Protein Interaction Domains and Motifs ,Protein Interaction Maps ,Adaptor Proteins, Signal Transducing ,Multidisciplinary ,biology ,Chemistry ,Eukaryotic transcription ,RNA-Binding Proteins ,Cell biology ,DNA-Binding Proteins ,Intrinsically Disordered Proteins ,Mutation ,biology.protein ,RNA Polymerase II ,Elongation ,Transcriptional Elongation Factors ,Protein Binding ,Transcription Factors - Abstract
Organized by unstructured motifs The high degree of conservation in protein sequences thought to be unstructured has hinted that these regions may have important biological functions. Although unstructured regions are widely viewed to be crucial for protein signaling, localization, and stability, their roles in many other settings have remained mysterious. Cermakova et al . discovered that prominent members of the transcription elongation machinery are linked through a network of interactions involving transcription elongation factor TFIIS N-terminal domains (TNDs) and conserved unstructured sequences called “TND-interacting motifs” (TIMs). The researchers found that mutation of a single TIM in a central organizing protein of this network abolished key protein interactions and induced widespread defects in transcription elongation dynamics. —DJ
- Published
- 2021