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Papers In Press, published online ahead of print August 10, 2000
Molecular and Cellular Biology, University of California, Davis, CA 95616
Corresponding Author: medahmus{at}ucdavis.edu
The fate of RNA polymerase II (RNAP 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 RNAP IIO to dephosphorylation, elongation complexes at defined positions on the Ad2-ML and HIV-1 templates were purified and their sensitivity to CTD phosphatase determined. Purified elongation complexes treated with 1% Sarkosyl and paused at U14/G16 on an HIV-1 template and 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 LTR and Ad2-MLP 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.
J. Biol. Chem, 10.1074/jbc.M005898200
Submitted on July 5, 2000
Accepted on August 9, 2000
CTD Phosphatase Sensitivity of RNA Polymerase II in Early Elongation Complexes on the HIV-1 and Ad2 Major Late Templates
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