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Expanding the SRI domain family: A common scaffold for binding the phosphorylated C-terminal domain of RNA polymerase II

Authors
Type
Published Article
Journal
FEBS Letters
Publisher
Wiley (John Wiley & Sons)
Publication Date
Oct 22, 2014
Volume
588
Issue
23
Pages
4431–4437
Identifiers
DOI: 10.1016/j.febslet.2014.10.014
OAI: oai:HAL:hal-01084875v1
Source
USPC - SET - SVS
Keywords
License
Green
External links

Abstract

The SRI domain is a small three-helix domain originally discovered near the C-terminus of both histonemethyltransferase SETD2 and helicase RECQL5. The SRI domain binds to the C-terminal repeatdomain of the largest subunit of RNA polymerase II, allowing SETD2 and RECQL5 to regulate variousmechanisms associated with RNA transcription. Using original tools to detect common patterns indistantly related sequences, we have identified SRI domains in several additional proteins, mostof which are involved in RNA metabolism. Combining sequence analysis with structural prediction,we show that this domain family is more diverse than previously thought and we predict criticalstructural and functional features.

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