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Papers In Press, published online ahead of print January 16, 2001
J. Biol. Chem, 10.1074/jbc.M010975200
Submitted on December 5, 2000
Revised on January 16, 2001
Accepted on January 15, 2001
Biochemistry & Molecular Biology, NJ Medical School-UMDNJ, Newark, NJ 07103-2714
Corresponding Author: peeryts{at}umdnj.edu
CDK7, CDK8 and CDK9 are cyclin-dependent kinases (CDKs) that phosphorylate the carboxy-terminal domain (CTD) of RNA polymerase II. They have distinct functions in transcription. Since the three CDKs target only serine-5 in the heptad repeat of model CTD substrates containing various numbers of repeats, we tested the hypothesis that the kinases differ in their ability to phosphorylate CTD heptad arrays. Our data show that the kinases display different preferences for phosphorylating individual heptads in a synthetic CTD substrate containing three heptamer repeats and specific regions of the CTD in glutathione S-transferase (GST) fusion proteins. They also exhibit differences in their ability to phosphorylate a synthetic CTD peptide that contains Ser-2-PO4. This phosphorylated peptide is a poor substrate for CDK9 complexes. CDK8 and CDK9 complexes bound to viral activators E1A and Tat respectively, target only serine 5 for phosphorylation in the CTD peptides and binding to the viral activators does not change the substrate preference of these kinases. These results imply that the display of different CTD heptads during transcription, as well as their phosphorylation state, can affect their phosphorylation by the different transcription-associated CDKs.
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