{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,2,23]],"date-time":"2026-02-23T19:19:32Z","timestamp":1771874372598,"version":"3.50.1"},"reference-count":40,"publisher":"Oxford University Press (OUP)","issue":"15","license":[{"start":{"date-parts":[[2016,11,10]],"date-time":"2016-11-10T00:00:00Z","timestamp":1478736000000},"content-version":"vor","delay-in-days":822,"URL":"http:\/\/creativecommons.org\/licenses\/by-nc\/4.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2014,9,2]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>Rrd1p (resistance to rapamycin deletion 1) has been previously implicated in controlling transcription of rapamycin-regulated genes in response to rapamycin treatment. Intriguingly, we show here that Rrd1p associates with the coding sequence of a galactose-inducible and rapamycin non-responsive GAL1 gene, and promotes the association of RNA polymerase II with GAL1 in the absence of rapamycin treatment following transcriptional induction. Consistently, nucleosomal disassembly at GAL1 is impaired in the absence of Rrd1p, and GAL1 transcription is reduced in the \u0394rrd1 strain. Likewise, Rrd1p associates with the coding sequences of other rapamycin non-responsive and inducible GAL genes to promote their transcription in the absence of rapamycin treatment. Similarly, inducible, but rapamycin-responsive, non-GAL genes such as CTT1, STL1 and CUP1 are also regulated by Rrd1p. However, transcription of these inducible GAL and non-GAL genes is not altered in the absence of Rrd1p when the steady-state is reached after long transcriptional induction. Consistently, transcription of the constitutively active genes is not changed in the \u0394rrd1 strain. Taken together, our results demonstrate a new function of Rrd1p in stimulation of initial rounds of transcription, but not steady-state\/constitutive transcription, of both rapamycin-responsive and non-responsive genes independently of rapamycin treatment.<\/jats:p>","DOI":"10.1093\/nar\/gku703","type":"journal-article","created":{"date-parts":[[2014,8,12]],"date-time":"2014-08-12T07:13:50Z","timestamp":1407827630000},"page":"9892-9907","source":"Crossref","is-referenced-by-count":11,"title":["Rrd1p, an RNA polymerase II-specific prolyl isomerase and activator of phosphoprotein phosphatase, promotes transcription independently of rapamycin response"],"prefix":"10.1093","volume":"42","author":[{"given":"Rwik","family":"Sen","sequence":"first","affiliation":[{"name":"Department of Biochemistry and Molecular Biology, Southern Illinois University School of Medicine, Carbondale, IL 62901, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Shivani","family":"Malik","sequence":"additional","affiliation":[{"name":"Department of Biochemistry and Molecular Biology, Southern Illinois University School of Medicine, Carbondale, IL 62901, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Sarah","family":"Frankland-Searby","sequence":"additional","affiliation":[{"name":"Department of Biochemistry and Molecular Biology, Southern Illinois University School of Medicine, Carbondale, IL 62901, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Bhawana","family":"Uprety","sequence":"additional","affiliation":[{"name":"Department of Biochemistry and Molecular Biology, Southern Illinois University School of Medicine, Carbondale, IL 62901, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Shweta","family":"Lahudkar","sequence":"additional","affiliation":[{"name":"Department of Biochemistry and Molecular Biology, Southern Illinois University School of Medicine, Carbondale, IL 62901, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Sukesh R.","family":"Bhaumik","sequence":"additional","affiliation":[{"name":"Department of Biochemistry and Molecular Biology, Southern Illinois University School of Medicine, Carbondale, IL 62901, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"286","published-online":{"date-parts":[[2014,8,11]]},"reference":[{"key":"2019070601434552900_B1","doi-asserted-by":"crossref","first-page":"6349","DOI":"10.1074\/jbc.M507760200","article-title":"The protein phosphatase 2A phosphatase activator is a novel peptidyl-prolyl cis\/trans-isomerase","volume":"281","author":"Jordens","year":"2006","journal-title":"J. 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