Molecular and Cellular Biology, July 2001, p. 4089-4096, Vol. 21, No. 13
Department of Molecular Genetics, Albert
Einstein College of Medicine, Bronx, New York
10461,1 and Department of Biology,
Sinsheimer Labs, University of California at Santa Cruz, Santa Cruz,
California 950642
Received 17 January 2001/Returned for modification 13 February
2001/Accepted 9 April 2001
BUR1, which was previously identified by a selection
for mutations that have general effects on transcription in
Saccharomyces cerevisiae, encodes a cyclin-dependent kinase
that is essential for viability, but none of its substrates have been
identified to date. Using an unbiased biochemical approach, we have
identified the carboxy-terminal domain (CTD) of Rpb1, the largest
subunit of RNA polymerase II, as a Bur1 substrate. Phosphorylation of Rpb1 by Bur1 is likely to be physiologically relevant, since
bur1 mutations interact genetically with rpb1
CTD truncations and with mutations in other genes involved in CTD
function. Several genetic interactions are presented, implying a role
for Bur1 during transcriptional elongation. These results identify Bur1
as a fourth S. cerevisiae CTD kinase and provide striking
functional similarities between Bur1 and metazoan P-TEFb.
0270-7306/01/$04.00+0 DOI: 10.1128/MCB.21.13.4089-4096.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.
Phosphorylation of the RNA Polymerase II
Carboxy-Terminal Domain by the Bur1 Cyclin-Dependent Kinase

*
Corresponding author. Mailing address: Department of
Molecular Genetics, Albert Einstein College of Medicine, 1300 Morris Park Ave., Bronx, NY 10461. Phone: (718) 430-2181. Fax: (718) 430-8778. E-mail: prelich{at}aecom.yu.edu.
Present address: Department of Cell Biology, Albert Einstein
College of Medicine, Bronx, NY 10461.
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