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Originally published In Press as doi:10.1074/jbc.M005898200 on August 10, 2000

J. Biol. Chem., Vol. 275, Issue 42, 32430-32437, October 20, 2000
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C-terminal Domain Phosphatase Sensitivity of RNA Polymerase II in Early Elongation Complexes on the HIV-1 and Adenovirus 2 Major Late Templates*

Nicholas F. Marshall and Michael E. DahmusDagger

From the Section of Molecular and Cellular Biology, Division of Biological Sciences, University of California, Davis, California 95616

The fate of RNA polymerase II in early elongation complexes is under the control of factors that regulate and respond to the phosphorylation state of the C-terminal domain (CTD). Phosphorylation of the CTD protects early elongation complexes from negative transcription elongation factors such as NELF, DSIF, and factor 2. To understand the relationship between transcript elongation and the sensitivity of RNA polymerase IIO to dephosphorylation, elongation complexes at defined positions on the Ad2-ML and human immunodeficiency virus type 1 (HIV-1) templates were purified, and their sensitivity to CTD phosphatase was determined. Purified elongation complexes treated with 1% Sarkosyl and paused at U14/G16 on an HIV-1 template and at G11 on the Ad2-ML template are equally sensitive to dephosphorylation by CTD phosphatase. Multiple elongation complexes paused at more promoter distal sites are more resistant to dephosphorylation than are U14/G16 and G11 complexes. The HIV-1 long terminal repeat and adenovirus 2 major late promoter do not appear to differentially influence the CTD phosphatase sensitivity of stringently washed complexes. Subsequent elongation by 1% Sarkosyl-washed U14/G16 complexes is unaffected by prior CTD phosphatase treatment. This result is consistent with the hypothesis that CTD phosphatase requires the presence of specific elongation factors to propagate a negative effect on transcript elongation. The action of CTD phosphatase on elongation complexes is inhibited by HIV-1 Tat protein. This observation is consistent with the idea that Tat suppression of CTD phosphatase plays a role in transactivation.

* This work was supported by National Institutes of Health Grant GM-33300 (to M. E. D.) and National Research Service Award Fellowship GM18952 (to N. F. M.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger To whom correspondence should be addressed. Tel.: 530-752-3551; Fax: 530-752-3085; E-mail: medahmus@ucdavis.edu.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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