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Papers In Press, published online ahead of print January 18, 2001
J. Biol. Chem, 10.1074/jbc.M007901200
Submitted on August 29, 2000
Revised on January 18, 2001
Accepted on January 17, 2001

HIV-1 Tat protein interacts with mammalian capping enzyme and stimulates capping of TAR RNA

Ya-Lin Chiu, Elizabeth Coronel, C. Kiong Ho, Stewart Shuman, and Tariq M. Rana

Pharmacology, University of Medicine and Dentistry of New Jersey, Piscataway, NJ 08854

Corresponding Author: rana{at}umdnj.edu

HIV gene expression is subject to a transcriptional checkpoint whereby negative transcription elongation factors induce an elongation block that is overcome by HIV Tat protein in conjunction with P-TEFb. P-TEFb is a cyclin-dependent kinase that catalyzes Tat-dependent phosphorylation of Ser5 of the Pol II CTD. Ser5 phosphorylation confers on the CTD the ability to recruit the mammalian mRNA capping enzyme (Mce1) and stimulate its guanylyltransferase activity. Here we show that Tat spearheads a second and novel pathway of capping enzyme recruitment and activation via a direct physical interaction between the C-terminal domain of Tat and Mce1. Tat stimulates the guanylyltransferase and triphosphatase activities of Mce1 and thereby enhances the otherwise low efficiency of cap formation on a TAR stem-loop RNA. Our findings suggest that multiple mechanisms exist for coupling transcription elongation and mRNA processing.


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