Sds3Sds3-like |
) |
|---|
| SMART accession number: | SM01401
|
|---|
| Description: |
Repression of gene transcription is mediated by histone deacetylases containing repressor-co-repressor complexes, which are recruited to promoters of target genes via interactions with sequence-specific transcription factors. The co-repressor complex contains a core of at least seven proteins PMID:15451426. This family represents the conserved region found in Sds3, Dep1 and BRMS1-homologue p40 proteins. |
|---|
| Interpro abstract (IPR013907): |
Repression of gene transcription is mediated by histone deacetylases containing repressor-co-repressor complexes, which are recruited to promoters of target genes via interactions with sequence-specific transcription factors. The co-repressor complex contains a core of at least seven proteins [ (PUBMED:15451426) ]. This entry represents the conserved region found in Sds3, Dep1 and BRMS1-homologue p40 proteins.
|
|---|
| Family alignment: |
|
|---|
There are 0 Sds3 domains in 0 proteins in SMART's nrdb database.
Click on the following links for more information.
Cellular role (predicted cellular role)
Cellular role: transcription
Literature (relevant references for this domain)
Primary literature is listed below; Automatically-derived, secondary literature is also avaliable.
- Nikolaev AY, Papanikolaou NA, Li M, Qin J, Gu W
- Identification of a novel BRMS1-homologue protein p40 as a component of themSin3A/p33(ING1b)/HDAC1 deacetylase complex.
- Biochem Biophys Res Commun. 2004; 323: 1216-22
- Display abstract
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.
Links (links to other resources describing this domain)
