Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

The structure of an Iws1/Spt6 complex reveals an interaction domain conserved in TFIIS, Elongin A and Med26.

The EMBO journal - 1 Dec 2010

Diebold Marie-Laure, Koch Michael, Loeliger Erin, Cura Vincent, Winston Fred, Cavarelli Jean, Romier Christophe

Abstract excerpt

Binding of elongation factor Spt6 to Iws1 provides an effective means for coupling eukaryotic mRNA synthesis, chromatin remodelling and mRNA export. We show that an N-terminal region of Spt6 (Spt6N) is responsible for interaction with Iws1. The crystallographic structures of Encephalitozoon cuniculi Iws1 and the Iws1/Spt6N complex reveal two conserved binding subdomains in Iws1. The first subdomain (one HEAT...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Crystallography, X-Ray
Share to Fungal Proteins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Point Mutation

Share to Protein Interaction Domains and Motifs

Share to Protein Structure, Tertiary

Share to Sequence Alignment

Share to Transcription, Genetic

Share to Transcriptional Elongation Factors

Source

Open in PubMed Open full text

Identifiers

PMID: 21057455
DOI: 10.1038/emboj.2010.272
PMCID: PMC3020637

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026. Manifest publication-graph-cohort-2026-09-05.1.

Source receipt: pubmed, retrieved 5 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The structure of an Iws1/Spt6 complex reveals an interaction domain conserved in TFIIS, Elongin A and Med26.PMID 21057455Read ↗

Essential histone chaperones collaborate to regulate transcription and chromatin integrity.Semantic proximity Read ↗

Suppressor mutations that make the essential transcription factor Spn1/Iws1 dispensable in <i>Saccharomyces cerevisiae</i>Semantic proximity Read ↗

The interaction between the Spt6-tSH2 domain and Rpb1 affects multiple functions of RNA Polymerase II.Semantic proximity Read ↗

Structural basis for Spt5-mediated recruitment of the Paf1 complex to chromatin.Semantic proximity Read ↗

Structure and biological importance of the Spn1-Spt6 interaction, and its regulatory role in nucleosome binding.Semantic proximity Read ↗

A ubiquitous disordered protein interaction module orchestrates transcription elongation.Semantic proximity Read ↗

TFIID TAF6-TAF9 complex formation involves the HEAT repeat-containing C-terminal domain of TAF6 and is modulated by TAF5 protein.Semantic proximity Read ↗

Spt5's central KOW domains and the Pol II stalk collaborate to regulate chromatin and 3'-end processing in Saccharomyces cerevisiae.Semantic proximity Read ↗

Evidence that Spt4, Spt5, and Spt6 control transcription elongation by RNA polymerase II in Saccharomyces cerevisiae.Semantic proximity Read ↗

OsARP6 Is Involved in Internode Elongation by Regulating Cell-Cycle-Related Genes.Semantic proximity Read ↗

RNA polymerase II elongation factors Spt4p and Spt5p play roles in transcription elongation by RNA polymerase I and rRNA processing.Semantic proximity Read ↗

Subunits of the yeast SWI/SNF complex are members of the actin-related protein (ARP) family.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.