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Regulation of P-TEFb elongation complex activity by CDK9 acetylation

DC FieldValueLanguage
dc.contributor.author윤호근-
dc.date.accessioned2014-12-21T17:12:31Z-
dc.date.available2014-12-21T17:12:31Z-
dc.date.issued2007-
dc.identifier.issn0270-7306-
dc.identifier.urihttps://ir.ymlib.yonsei.ac.kr/handle/22282913/97150-
dc.description.abstractP-TEFb, comprised of CDK9 and a cyclin T subunit, is a global transcriptional elongation factor important for most RNA polymerase II (pol II) transcription. P-TEFb facilitates transcription elongation in part by phosphorylating Ser2 of the heptapeptide repeat of the carboxy-terminal domain (CTD) of the largest subunit of pol II. Previous studies have shown that P-TEFb is subjected to negative regulation by forming an inactive complex with 7SK small RNA and HEXIM1. In an effort to investigate the molecular mechanism by which corepressor N-CoR mediates transcription repression, we identified HEXIM1 as an N-CoR-interacting protein. This finding led us to test whether the P-TEFb complex is regulated by acetylation. We demonstrate that CDK9 is an acetylated protein in cells and can be acetylated by p300 in vitro. Through both in vitro and in vivo assays, we identified lysine 44 of CDK9 as a major acetylation site. We present evidence that CDK9 is regulated by N-CoR and its associated HDAC3 and that acetylation of CDK9 affects its ability to phosphorylate the CTD of pol II. These results suggest that acetylation of CDK9 is an important posttranslational modification that is involved in regulating P-TEFb transcriptional elongation function.-
dc.description.statementOfResponsibilityopen-
dc.format.extent4641~4651-
dc.relation.isPartOfMOLECULAR AND CELLULAR BIOLOGY-
dc.rightsCC BY-NC-ND 2.0 KR-
dc.rights.urihttps://creativecommons.org/licenses/by-nc-nd/2.0/kr/-
dc.titleRegulation of P-TEFb elongation complex activity by CDK9 acetylation-
dc.typeArticle-
dc.contributor.collegeCollege of Medicine (의과대학)-
dc.contributor.departmentDept. of Biochemistry & Molecular Biology (생화학,분자생물학)-
dc.contributor.googleauthorJunjiang Fu-
dc.contributor.googleauthorHo-Geun Yoon-
dc.contributor.googleauthorJiemin Wong-
dc.contributor.googleauthorJun Qin-
dc.identifier.doi10.1128/MCB.00857-06-
dc.admin.authorfalse-
dc.admin.mappingfalse-
dc.contributor.localIdA02625-
dc.relation.journalcodeJ02243-
dc.identifier.eissn1098-5549-
dc.contributor.alternativeNameYoon, Ho Geun-
dc.contributor.affiliatedAuthorYoon, Ho Geun-
dc.rights.accessRightsfree-
dc.citation.volume27-
dc.citation.number13-
dc.citation.startPage4641-
dc.citation.endPage4651-
dc.identifier.bibliographicCitationMOLECULAR AND CELLULAR BIOLOGY, Vol.27(13) : 4641-4651, 2007-
Appears in Collections:
1. College of Medicine (의과대학) > Dept. of Biochemistry and Molecular Biology (생화학-분자생물학교실) > 1. Journal Papers

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