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Expanding the SRI domain family: A common scaffold for binding the phosphorylated C‐terminal domain of RNA polymerase II
Author(s) -
Rebehmed Joseph,
Revy Patrick,
Faure Guilhem,
de Villartay Jean-Pierre,
Callebaut Isabelle
Publication year - 2014
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2014.10.014
Subject(s) - rna helicase a , rna polymerase ii , helicase , biology , rna polymerase ii holoenzyme , genetics , polymerase , microbiology and biotechnology , computational biology , rna polymerase , histone , transcription (linguistics) , rna , gene , gene expression , promoter , linguistics , philosophy
The SRI domain is a small three‐helix domain originally discovered near the C‐terminus of both histone methyltransferase SETD2 and helicase RECQL5. The SRI domain binds to the C‐terminal repeat domain of the largest subunit of RNA polymerase II, allowing SETD2 and RECQL5 to regulate various mechanisms associated with RNA transcription. Using original tools to detect common patterns in distantly related sequences, we have identified SRI domains in several additional proteins, most of 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 critical structural and functional features.