{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,6,10]],"date-time":"2026-06-10T15:31:19Z","timestamp":1781105479583,"version":"3.54.1"},"reference-count":60,"publisher":"National Academy of Sciences","issue":"9","content-domain":{"domain":["www.pnas.org"],"crossmark-restriction":true},"short-container-title":["Proc. Natl. Acad. Sci. U.S.A."],"published-print":{"date-parts":[[2002,4,30]]},"abstract":"<jats:p>\n                    The general transcription factor TFIID facilitates recruitment of the transcription machinery to gene promoters and regulates initiation of transcription by RNA polymerase II. hTAF\n                    <jats:sub>II<\/jats:sub>\n                    130, a component of TFIID, interacts with and serves as a coactivator for multiple transcriptional regulatory proteins, including Sp1 and CREB. A yeast two-hybrid screen has identified an interaction between hTAF\n                    <jats:sub>II<\/jats:sub>\n                    130 and heterochromatin protein 1 (HP1), a chromatin-associated protein whose function has been implicated in gene silencing. We find that hTAF\n                    <jats:sub>II<\/jats:sub>\n                    130 associates with HP1 in an isoform-specific manner: HP1\u03b1 and HP1\u03b3 bind to hTAF\n                    <jats:sub>II<\/jats:sub>\n                    130, but not HP1\u03b2. In addition, we show that endogenous hTAF\n                    <jats:sub>II<\/jats:sub>\n                    130 and components of TFIID in HeLa nuclear extracts associate with glutathione\n                    <jats:italic>S<\/jats:italic>\n                    -transferase-HP1\u03b1 and -HP1\u03b3. hTAF\n                    <jats:sub>II<\/jats:sub>\n                    130 possesses a pentapeptide HP1-binding motif, and mutation of the hTAF\n                    <jats:sub>II<\/jats:sub>\n                    130 HP1 box compromises the interaction of hTAF\n                    <jats:sub>II<\/jats:sub>\n                    130 with HP1. We demonstrate that Gal4-HP1 proteins interfere with hTAF\n                    <jats:sub>II<\/jats:sub>\n                    130-mediated activation of transcription. Our results suggest that HP1\u03b1 and HP1\u03b3 associate with hTAF\n                    <jats:sub>II<\/jats:sub>\n                    130 to mediate repression of transcription, supporting a new model of transcriptional repression involving a specific interaction between a component of TFIID and chromatin.\n                  <\/jats:p>","DOI":"10.1073\/pnas.092025499","type":"journal-article","created":{"date-parts":[[2002,7,28]],"date-time":"2002-07-28T18:26:28Z","timestamp":1027880788000},"page":"5919-5924","update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":56,"title":["Isoform-specific interaction of HP1 with human TAF\n                    <sub>II<\/sub>\n                    130"],"prefix":"10.1073","volume":"99","author":[{"given":"Milo F.","family":"Vassallo","sequence":"first","affiliation":[{"name":"Department of Microbiology and Kaplan Comprehensive Cancer Center, New York University School of Medicine, New York, NY 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