|PROSITE documentation PDOC51518 [for PROSITE entry PS51518]|
Eukaryotic SGF29 is a component of histone acetyltransferase (HAT) complexes TATA-binding protein-free TAF-containing (TFTC) and SPT3-TAF9-GCN5-acetyltransferase (STAGA) or SPT-ADA-GCN5-acetyltransferase (SAGA) . The SGF29 C-terminal domain contains a double Tudor-like motif that selectively binds the H3K4me2/3 lysine methylation site on the N terminus of histone H3 [2,3].
Each Tudor domain consists of five twisted anti-parallel β strands forming a typical barrel-like fold (see <PDB:3MEA>). The tandem Tudor domains tightly pack against each other face-to-face with each Tudor domain harboring a negatively charged pocket accommodating the first residue alanine and methylated K4 residue of histone H3, respectively .
The profile we developed covers the entire SGF29 C-terminal domain.Last update:
December 2011 / Profile and text revised.
PROSITE method (with tools and information) covered by this documentation:
|1||Authors||Kurabe N. Katagiri K. Komiya Y. Ito R. Sugiyama A. Kawasaki Y. Tashiro F.|
|Title||Deregulated expression of a novel component of TFTC/STAGA histone acetyltransferase complexes, rat SGF29, in hepatocellular carcinoma: possible implication for the oncogenic potential of c-Myc.|
|2||Authors||Vermeulen M. Eberl H.C. Matarese F. Marks H. Denissov S. Butter F. Lee K.K. Olsen J.V. Hyman A.A. Stunnenberg H.G. Mann M.|
|Title||Quantitative interaction proteomics and genome-wide profiling of epigenetic histone marks and their readers.|
|3||Authors||Bian C. Xu C. Ruan J. Lee K.K. Burke T.L. Tempel W. Barsyte D. Li J. Wu M. Zhou B.O. Fleharty B.E. Paulson A. Allali-Hassani A. Zhou J.-Q. Mer G. Grant P.A. Workman J.L. Zang J. Min J.|
|Title||Sgf29 binds histone H3K4me2/3 and is required for SAGA complex recruitment and histone H3 acetylation.|
|Source||EMBO J. 30:2829-2842(2011).|