A ubiquitous disordered protein interaction module orchestrates transcription elongation
| Autor: | 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, Katerina Cermakova |
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| Jazyk: | angličtina |
| Rok vydání: | 2021 |
| Předmět: |
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 |
| Zdroj: | Science |
| Popis: | 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 |
| Databáze: | OpenAIRE |
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