Rtr1 is a CTD phosphatase that regulates RNA polymerase II during the transition from serine 5 to serine 2 phosphorylation.
Rtr1 is a CTD phosphatase that regulates RNA polymerase II during the transition from serine 5 to serine 2 phosphorylation.
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DOI:
10.1016/j.molcel.2009.02.025
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发表时间:
2009-04-24
期刊:
影响因子:
16
通讯作者:
Washburn, Michael P.
中科院分区:
文献类型:
--
作者:
Mosley, Amber L.;Pattenden, Samantha G.;Carey, Michael;Venkatesh, Swaminathan;Gilmore, Joshua M.;Florens, Laurence;Workman, Jerry L.;Washburn, Michael P.
Messenger RNA processing is coupled to RNA Polymerase II (RNAPII) transcription through coordinated recruitment of accessory proteins to the Rpb1 C-terminal domain (CTD). Dynamic changes in CTD phosphorylation during transcription elongation are responsible for their recruitment, with serine 5 phosphorylation (S5-P) occurring towards the 5’ end of genes and serine 2 phosphorylation (S2-P) occurring towards the 3’ end. The proteins responsible for regulation of the transition state between S5-P and S2-P CTD remain elusive. We show that a conserved protein of unknown function, Rtr1, localizes within coding regions, with maximum levels of enrichment occurring between the peaks of S5-P and S2-P RNAPII. Upon deletion of Rtr1, the S5-P form of RNAPII accumulates in both whole cell extracts and throughout coding regions; additionally, RNAPII transcription is decreased and termination defects are observed. Functional characterization of Rtr1 reveals its role as a CTD phosphatase essential for the S5- to S2- P transition.
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影响因子:
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作者:
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通讯作者:
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DOI:
10.1073/pnas.0804424105
发表时间:
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影响因子:
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