Phosphorylation of the RNA Polymerase II Carboxy-Terminal Domain by the Bur1 Cyclin-Dependent Kinase
- 1 July 2001
- journal article
- research article
- Published by Taylor & Francis in Molecular and Cellular Biology
- Vol. 21 (13), 4089-4096
- https://doi.org/10.1128/mcb.21.13.4089-4096.2001
Abstract
BUR1, which was previously identified by a selection for mutations that have general effects on transcription inSaccharomyces 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, sincebur1 mutations interact genetically with rpb1CTD 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.Keywords
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