ArticleProtein science : a publication of the Protein Society2006
Structure of the Sir3 protein bromo adjacent homology (BAH) domain from S. cerevisiae at 1.95 A resolution.
Article in Protein science : a publication of the Protein Society, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed.
- Transcriptional silencing in Saccharomyces cerevisiae: known unknowns.Epigenetics & chromatin · 2024Review
- Histone Readers and Their Roles in Cancer.Cancer treatment and research · 2023Article
- The Nuts and Bolts of Transcriptionally Silent Chromatin in Saccharomyces cerevisiae.Genetics · 2016Review
- Two Loops Undergoing Concerted Dynamics Regulate the Activity of the ASH1L Histone Methyltransferase.Biochemistry · 2015Article
- Nα-acetylated Sir3 stabilizes the conformation of a nucleosome-binding loop in the BAH domain.Nature structural & molecular biology · 2013Article
- The role of the nucleosome acidic patch in modulating higher order chromatin structure.Journal of the Royal Society, Interface · 2013Review
- Ascending the nucleosome face: recognition and function of structured domains in the histone H2A-H2B dimer.Biochimica et biophysica acta · 2012Article
- Structural basis of silencing: Sir3 BAH domain in complex with a nucleosome at 3.0 Å resolution.Science (New York, N.Y.) · 2011Article
- Structural basis for the role of the Sir3 AAA+ domain in silencing: interaction with Sir4 and unmethylated histone H3K79.Genes & development · 2011Article
- The conserved bromo-adjacent homology domain of yeast Orc1 functions in the selection of DNA replication origins within chromatin.Genes & development · 2010Article
- Silent information regulator 3: the Goldilocks of the silencing complex.Genes & development · 2010Review
- Review
- Phylogenetic conservation and homology modeling help reveal a novel domain within the budding yeast heterochromatin protein Sir1.Molecular and cellular biology · 2009Article
- Compensatory interactions between Sir3p and the nucleosomal LRS surface imply their direct interaction.PLoS genetics · 2008Article
- Sir3-nucleosome interactions in spreading of silent chromatin in Saccharomyces cerevisiae.Molecular and cellular biology · 2008Article
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4 authors.
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Abstract
Sir3p is a silent-information-regulator (SIR) protein required for the assembly of a transcriptionally "silent" chromatin structure at telomeres and the cryptic HM mating-type loci in Saccharomyces cerevisiae. Sir3p contains a putative "bromo adjacent homology" (BAH) domain at its N terminus that shares strong sequence similarity with the BAH domain of a subunit of the origin recognition complex (ORC), Orc1p. The Orc1p-BAH domain forms a well-defined complex with the ORC interaction region (OIR) of another Sir protein, Sir1p, which targets formation of silent chromatin to the HM-loci. Interestingly, despite sequence similarity of the Sir3p and Orc1p BAH domains and Sir3p's established importance in silencing, Sir3p does not bind the Sir1p-OIR. Here we report the 1.95 A resolution crystal structure of the Sir3p-BAH domain. The structure reveals two key features that can account for Sir3p-BAH domain's inability to interact with Sir1p. First, several Orc1p-BAH domain residues known to directly contact Sir1p are altered in the Sir3p-BAH domain. Second, a critical OIR-binding pocket present on the surface of the Orc1p-BAH domain is "filled" in the Sir3p-BAH domain structure, potentially making it inaccessible to Sir1p. These findings imply that the Sir3p-BAH domain structure has evolved for functions distinct from those of the Orc1p-BAH domain.
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