Predicted cellular role

Primary literature for the Sds3 domain is listed below.

Identification of a novel BRMS1-homologue protein p40 as a component of themSin3A/p33(ING1b)/HDAC1 deacetylase complex.

Nikolaev AY, Papanikolaou NA, Li M, Qin J, Gu W
Biochem Biophys Res Commun. 2004; 323: 1216-22

Repression of gene transcription is mediated by histone deacetylases containingrepressor-co-repressor complexes, which are recruited to promoters of targetgenes via interactions with sequence-specific transcription factors. Themammalian Sin3A co-repressor complex contains a core of at least seven proteinsincluding the pRb-interacting protein RBP1 and a putative tumor suppressorp33(ING1b). By biochemical purification and mass spectrometry, we have identifieda novel component p40 from this complex. p40 bears homology to both yeast Sds3, acomponent of yeast histone deacetylase complexes, and its mammalian homologuemSds3. The p40-associated complex purified from human cells shows a stronghistone deacetylase activity. When tethered to a Gal-DNA binding domain, theGal-p40 is able to significantly repress transcription of a Gal-luciferasepromoter. Interestingly, database analysis reveals that p40 is also highlyhomologous to BRMS1, a breast carcinoma metastasis suppressor, and overexpressionof p40 in human cells can significantly inhibit cell growth. Thus, our dataindicate that p40 may be critically involved in transcription repression of cell growth-associated gene expression by recruiting the HDAC1 deacetylase complex.