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Originally published In Press as doi:10.1074/jbc.M500424200 on February 14, 2005

J. Biol. Chem., Vol. 280, Issue 16, 16360-16367, April 22, 2005
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HEXIM2, a HEXIM1-related Protein, Regulates Positive Transcription Elongation Factor b through Association with 7SK*{boxs}

Sarah A. Byers{ddagger}, Jason P. Price§, Jeffrey J. Cooper§, Qintong Li§, and David H. Price§

From the {ddagger}Molecular Biology Program and §Department of Biochemistry, University of Iowa, Iowa City, Iowa 52242

The kinase activity of positive transcription elongation factor b (P-TEFb), composed of cyclin-dependent kinase 9 and cyclin T1 or T2, is required for the transition of RNA polymerase II into productive elongation. P-TEFb activity has been shown to be negatively regulated by association with the small nuclear RNA 7SK and the HEXIM1 protein. Here, we characterize HEXIM2, a previously predicted protein with sequence similarity to HEXIM1. HEXIM2 is expressed in HeLa and Jurkat cells, and glycerol gradient analysis and immunoprecipitations indicate that HEXIM2, like HEXIM1, has a regulated association with P-TEFb. As HEXIM1 is knocked down, HEXIM2 functionally compensates for its association with P-TEFb. Electrophoretic mobility shift assays and in vitro kinase assays demonstrate that HEXIM2 forms complexes containing 7SK and P-TEFb and, in conjunction with 7SK, inhibits P-TEFb kinase activity. Our results provide strong evidence that HEXIM2 is a regulator of P-TEFb function. Furthermore, our results support the idea that the utilization of HEXIM1 or HEXIM2 to bind and inhibit P-TEFb can be differentially regulated in vivo.

Received for publication, January 12, 2005

* This work was supported by National Institutes of Health Grant GM35500. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

{boxs} The on-line version of this article (available at http://www.jbc.org) contains supplemental Fig. 1S.

To whom correspondence should be addressed: Dept. of Biochemistry, University of Iowa, 375 Newton Rd., Iowa City, IA 52242. Tel.: 319-335-7910; Fax: 319-384-4770; E-mail: david-price{at}uiowa.edu.


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