pubmed-article:16641491 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:16641491 | lifeskim:mentions | umls-concept:C0036025 | lld:lifeskim |
pubmed-article:16641491 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
pubmed-article:16641491 | lifeskim:mentions | umls-concept:C1412592 | lld:lifeskim |
pubmed-article:16641491 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
pubmed-article:16641491 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
pubmed-article:16641491 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
pubmed-article:16641491 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
pubmed-article:16641491 | lifeskim:mentions | umls-concept:C0205117 | lld:lifeskim |
pubmed-article:16641491 | lifeskim:mentions | umls-concept:C2699488 | lld:lifeskim |
pubmed-article:16641491 | lifeskim:mentions | umls-concept:C1334043 | lld:lifeskim |
pubmed-article:16641491 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
pubmed-article:16641491 | lifeskim:mentions | umls-concept:C2697616 | lld:lifeskim |
pubmed-article:16641491 | pubmed:issue | 5 | lld:pubmed |
pubmed-article:16641491 | pubmed:dateCreated | 2006-4-27 | lld:pubmed |
pubmed-article:16641491 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16641491 | pubmed:abstractText | 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. | lld:pubmed |
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pubmed-article:16641491 | pubmed:language | eng | lld:pubmed |
pubmed-article:16641491 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16641491 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:16641491 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16641491 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:16641491 | pubmed:month | May | lld:pubmed |
pubmed-article:16641491 | pubmed:issn | 0961-8368 | lld:pubmed |
pubmed-article:16641491 | pubmed:author | pubmed-author:DanzerJohn... | lld:pubmed |
pubmed-article:16641491 | pubmed:author | pubmed-author:KeckJames LJL | lld:pubmed |
pubmed-article:16641491 | pubmed:author | pubmed-author:FoxCatherine... | lld:pubmed |
pubmed-article:16641491 | pubmed:author | pubmed-author:HouZhonggangZ | lld:pubmed |
pubmed-article:16641491 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:16641491 | pubmed:volume | 15 | lld:pubmed |
pubmed-article:16641491 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:16641491 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:16641491 | pubmed:pagination | 1182-6 | lld:pubmed |
pubmed-article:16641491 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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pubmed-article:16641491 | pubmed:meshHeading | pubmed-meshheading:16641491... | lld:pubmed |
pubmed-article:16641491 | pubmed:year | 2006 | lld:pubmed |
pubmed-article:16641491 | pubmed:articleTitle | Structure of the Sir3 protein bromo adjacent homology (BAH) domain from S. cerevisiae at 1.95 A resolution. | lld:pubmed |
pubmed-article:16641491 | pubmed:affiliation | Department of Biomolecular Chemistry, University of Wisconsin School of Medicine and Public Health, Madison, Wisconsin 53706-1532, USA. | lld:pubmed |
pubmed-article:16641491 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:16641491 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
pubmed-article:16641491 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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