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Molecular and Cellular Biology, June 2009, p. 2925-2934, Vol. 29, No. 11
0270-7306/09/$08.00+0     doi:10.1128/MCB.01655-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

Functional Interaction of the Ess1 Prolyl Isomerase with Components of the RNA Polymerase II Initiation and Termination Machineries{triangledown}

Shankarling Krishnamurthy,1 Mohamed A. Ghazy,2 Claire Moore,2 and Michael Hampsey1*

Department of Biochemistry, Division of Nucleic Acids Enzymology, Robert Wood Johnson Medical School, 683 Hoes Lane, Piscataway, New Jersey 08854,1 Department of Molecular Biology and Microbiology, Tufts University School of Medicine, Boston, Massachusetts 021112

Received 23 October 2008/ Returned for modification 19 November 2008/ Accepted 19 March 2009

The C-terminal domain (CTD) of the largest subunit of RNA polymerase II (Pol II) is a reiterated heptad sequence (Tyr1-Ser2-Pro3-Thr4-Ser5-Pro6-Ser7) that plays a key role in the transcription cycle, coordinating the exchange of transcription and RNA processing factors. The structure of the CTD is flexible and undergoes conformational changes in response to serine phosphorylation and proline isomerization. Here we report that the Ess1 peptidyl prolyl isomerase functionally interacts with the transcription initiation factor TFIIB and with the Ssu72 CTD phosphatase and Pta1 components of the CPF 3'-end processing complex. The ess1A144T and ess1H164R mutants, initially described by Hanes and coworkers (Yeast 5:55-72, 1989), accumulate the pSer5 phosphorylated form of Pol II; confer phosphate, galactose, and inositol auxotrophies; and fail to activate PHO5, GAL10, and INO1 reporter genes. These mutants are also defective for transcription termination, but in vitro experiments indicate that this defect is not caused by altering the processing efficiency of the cleavage/polyadenylation machinery. Consistent with a role in initiation and termination, Ess1 associates with the promoter and terminator regions of the PMA1 and PHO5 genes. We propose that Ess1 facilitates pSer5-Pro6 dephosphorylation by generating the CTD structural conformation recognized by the Ssu72 phosphatase and that pSer5 dephosphorylation affects both early and late stages of the transcription cycle.

* Corresponding author. Mailing address: Department of Biochemistry, Robert Wood Johnson Medical School, 683 Hoes Lane West, Piscataway, NJ 08854. Phone: (732) 235-5888. Fax: (732) 235-5889. E-mail: michael.hampsey{at}umdnj.edu

{triangledown} Published ahead of print on 30 March 2009.

Molecular and Cellular Biology, June 2009, p. 2925-2934, Vol. 29, No. 11
0270-7306/09/$08.00+0     doi:10.1128/MCB.01655-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Yunokuchi, I., Fan, H., Iwamoto, Y., Araki, C., Yuda, M., Umemura, H., Harada, F., Ohkuma, Y., Hirose, Y. (2009). Prolyl isomerase Pin1 shares functional similarity with phosphorylated CTD interacting factor PCIF1 in vertebrate cells. GENES CELLS 14: 1105-1118 [Abstract] [Full Text]  


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