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PROSITE documentation PDOC51518 [for PROSITE entry PS51518]

SGF29 C-terminal domain profile





Description

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) [1]. 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 [3].

The profile we developed covers the entire SGF29 C-terminal domain.

Last update:

December 2011 / Profile and text revised.

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Technical section

PROSITE method (with tools and information) covered by this documentation:

SGF29_C, PS51518; SGF29 C-terminal domain profile  (MATRIX)


References

1AuthorsKurabe N. Katagiri K. Komiya Y. Ito R. Sugiyama A. Kawasaki Y. Tashiro F.
TitleDeregulated 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.
SourceOncogene 26:5626-5634(2007).
PubMed ID17334388
DOI10.1038/sj.onc.1210349

2AuthorsVermeulen 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.
TitleQuantitative interaction proteomics and genome-wide profiling of epigenetic histone marks and their readers.
SourceCell 142:967-980(2010).
PubMed ID20850016
DOI10.1016/j.cell.2010.08.020

3AuthorsBian 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.
TitleSgf29 binds histone H3K4me2/3 and is required for SAGA complex recruitment and histone H3 acetylation.
SourceEMBO J. 30:2829-2842(2011).
PubMed ID21685874
DOI10.1038/emboj.2011.193



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