{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,5,7]],"date-time":"2026-05-07T16:15:20Z","timestamp":1778170520664,"version":"3.51.4"},"reference-count":55,"publisher":"Cold Spring Harbor Laboratory","issue":"23","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Genes Dev."],"published-print":{"date-parts":[[2001,12,1]]},"abstract":"<jats:p>It is well established that acetylation of histone and nonhistone proteins is intimately linked to transcriptional activation. However, loss of acetyltransferase activity has also been shown to cause silencing defects, implicating acetylation in gene silencing. The something about silencing (Sas) 2 protein of <jats:italic>Saccharomyces cerevisiae<\/jats:italic>, a member of the MYST (<jats:underline>M<\/jats:underline>OZ,<jats:underline>Y<\/jats:underline>bf2\/Sas3, <jats:underline>S<\/jats:underline>as2, and <jats:underline>T<\/jats:underline>IP60) acetyltransferase family, promotes silencing at <jats:italic>HML<\/jats:italic> and telomeres. Here we identify a \u223c450-kD SAS complex containing Sas2p, Sas4p, and the tf2f-related Sas5 protein. Mutations in the conserved acetyl-CoA binding motif of Sas2p are shown to disrupt the ability of Sas2p to mediate the silencing at <jats:italic>HML<\/jats:italic> and telomeres, providing evidence for an important role for the acetyltransferase activity of the SAS complex in silencing. Furthermore, the SAS complex is found to interact with chromatin assembly factor Asf1p, and <jats:italic>asf1<\/jats:italic> mutants show silencing defects similar to mutants in the SAS complex. Thus, ASF1-dependent chromatin assembly may mediate the role of the SAS complex in silencing.<\/jats:p>","DOI":"10.1101\/gad.907201","type":"journal-article","created":{"date-parts":[[2002,7,26]],"date-time":"2002-07-26T23:59:15Z","timestamp":1027727955000},"page":"3155-3168","source":"Crossref","is-referenced-by-count":102,"title":["The yeast SAS (something about silencing) protein complex contains a MYST-type putative acetyltransferase and functions with chromatin assembly factor ASF1"],"prefix":"10.1101","volume":"15","author":[{"given":"Shigehiro","family":"Osada","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Ann","family":"Sutton","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Nemone","family":"Muster","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Christine E.","family":"Brown","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"suffix":"III","given":"John R.","family":"Yates","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Rolf","family":"Sternglanz","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Jerry L.","family":"Workman","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"246","published-online":{"date-parts":[[2001,12,1]]},"reference":[{"key":"2021111507523829000_15.23.3155.1","doi-asserted-by":"publisher","DOI":"10.1093\/emboj\/18.18.5108"},{"key":"2021111507523829000_15.23.3155.2","doi-asserted-by":"publisher","DOI":"10.1093\/nar\/25.17.3389"},{"key":"2021111507523829000_15.23.3155.3","doi-asserted-by":"publisher","DOI":"10.1016\/0092-8674(91)90049-5"},{"key":"2021111507523829000_15.23.3155.4","doi-asserted-by":"publisher","DOI":"10.1038\/ng0996-33"},{"key":"2021111507523829000_15.23.3155.5","doi-asserted-by":"publisher","DOI":"10.1016\/S0968-0004(99)01516-9"},{"key":"2021111507523829000_15.23.3155.6","doi-asserted-by":"crossref","first-page":"3308","DOI":"10.1128\/MCB.16.7.3308","article-title":"TFG\/TAF30\/ANC1, a component of the yeast SWI\/SNF complex that is similar to the leukemogenic proteins ENL and AF-9.","volume":"16","author":"Cairns","year":"1996","journal-title":"Mol. 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