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dc.contributor.authorLopes da Rosa Spiegler, Jessica
dc.contributor.authorBajaj, Vineeta
dc.contributor.authorSpoonamore, James
dc.contributor.authorKaufman, Paul D.
dc.date2022-08-11T08:08:23.000
dc.date.accessioned2022-08-23T15:53:01Z
dc.date.available2022-08-23T15:53:01Z
dc.date.issued2013-05-15
dc.date.submitted2013-06-05
dc.identifier.citationBioorg Med Chem Lett. 2013 May 15;23(10):2853-9. doi: 10.1016/j.bmcl.2013.03.112. <a href="http://dx.doi.org/10.1016/j.bmcl.2013.03.112">Link to article on publisher's site</a>
dc.identifier.issn0960-894X (Linking)
dc.identifier.doi10.1016/j.bmcl.2013.03.112
dc.identifier.pmid23587423
dc.identifier.urihttp://hdl.handle.net/20.500.14038/29269
dc.description.abstractThe histone acetyltransferase Rtt109 is the sole enzyme responsible for acetylation of histone H3 lysine 56 (H3K56) in fungal organisms. Loss of Rtt109 renders fungal cells extremely sensitive to genotoxic agents, and prevents pathogenesis in several clinically important species. Here, via a high throughput chemical screen of >300,000 compounds, we discovered a chemical inhibitor of Rtt109 that does not inhibit other acetyltransferase enzymes. This compound inhibits Rtt109 regardless of which histone chaperone cofactor protein (Asf1 or Vps75) is present, and appears to inhibit Rtt109 via a tight-binding, uncompetitive mechanism.
dc.language.isoen_US
dc.relation<a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&cmd=Retrieve&list_uids=23587423&dopt=Abstract">Link to Article in PubMed</a>
dc.relation.urlhttp://dx.doi.org/10.1016/j.bmcl.2013.03.112
dc.subjectHistone Acetyltransferases
dc.subjectSaccharomyces cerevisiae Proteins
dc.subjectCandida albicans
dc.subjectBiochemistry, Biophysics, and Structural Biology
dc.titleA small molecule inhibitor of fungal histone acetyltransferase Rtt109
dc.typeJournal Article
dc.source.journaltitleBioorganic and medicinal chemistry letters
dc.source.volume23
dc.source.issue10
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/faculty_pubs/15
dc.identifier.contextkey4199945
html.description.abstract<p>The histone acetyltransferase Rtt109 is the sole enzyme responsible for acetylation of histone H3 lysine 56 (H3K56) in fungal organisms. Loss of Rtt109 renders fungal cells extremely sensitive to genotoxic agents, and prevents pathogenesis in several clinically important species. Here, via a high throughput chemical screen of >300,000 compounds, we discovered a chemical inhibitor of Rtt109 that does not inhibit other acetyltransferase enzymes. This compound inhibits Rtt109 regardless of which histone chaperone cofactor protein (Asf1 or Vps75) is present, and appears to inhibit Rtt109 via a tight-binding, uncompetitive mechanism.</p>
dc.identifier.submissionpathfaculty_pubs/15
dc.contributor.departmentProgram in Molecular Medicine
dc.contributor.departmentProgram in Gene Function and Expression
dc.source.pages2853-9


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