D
IPR047288

SAGA-associated factor 29, first Tudor domain

InterPro entry
Short nameTudor_SGF29_rpt1
domain relationships

Description

This entry represents the first Tudor domain of SGF29 and similar eukaryotic proteins.

SAGA-associated factor 29 (SGF29) is a chromatin reader and a component of the transcription regulatory histone acetylation (HAT) complexes SAGA and SLIK
[2, 3]
. In the SAGA complex, SGF29 binds histone H3 that has been methylated at Lys-4 (H3K4me), and preferably binds the trimethylated form (H3K4me3)
[1]
. SGF29 also acts as a boundary, preventing the spread of heterochromatin into neighbouring genes
[4]
. SGF29 contains two Tudor domains.

References

1.Sgf29 binds histone H3K4me2/3 and is required for SAGA complex recruitment and histone H3 acetylation. Bian C, Xu C, Ruan J, Lee KK, Burke TL, Tempel W, Barsyte D, Li J, Wu M, Zhou BO, Fleharty BE, Paulson A, Allali-Hassani A, Zhou JQ, Mer G, Grant PA, Workman JL, Zang J, Min J. EMBO J. 30, 2829-42, (2011). View articlePMID: 21685874

2.Expanded lysine acetylation specificity of Gcn5 in native complexes. Grant PA, Eberharter A, John S, Cook RG, Turner BM, Workman JL. J. Biol. Chem. 274, 5895-900, (1999). View articlePMID: 10026213

3.Chd1 chromodomain links histone H3 methylation with SAGA- and SLIK-dependent acetylation. Pray-Grant MG, Daniel JA, Schieltz D, Yates JR 3rd, Grant PA. Nature 433, 434-8, (2005). View articlePMID: 15647753

4.The N-terminus and Tudor domains of Sgf29 are important for its heterochromatin boundary formation function. Kamata K, Goswami G, Kashio S, Urano T, Nakagawa R, Uchida H, Oki M. J. Biochem. 155, 159-71, (2014). View articlePMID: 24307402

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