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A ubiquitous disordered protein interaction module orchestrates transcription elongation
Author(s) -
Kateřina Čermáková,
Jonas Demeulemeester,
Vanda Lux,
Monika Nedomova,
Seth R. Goldman,
Eric A. Smith,
Pavel Srb,
R. Hexnerova,
Milan Fábry,
Marcela Mádlíková,
Magdaléna Hořejší,
Jan De Rijck,
Zeger Debyser,
Karen Adelman,
H. Courtney Hodges,
Václav Veverka
Publication year - 2021
Publication title -
science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 12.556
H-Index - 1186
eISSN - 1095-9203
pISSN - 0036-8075
DOI - 10.1126/science.abe2913
Subject(s) - elongation factor , microbiology and biotechnology , biology , rna polymerase ii , elongation , transcription factor , transcription (linguistics) , mediator , computational biology , rna , genetics , gene , promoter , gene expression , ribosome , linguistics , materials science , philosophy , ultimate tensile strength , metallurgy
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. Cermakovaet 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

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