Yeast Genetics and Molecular Biology 2002
University of Wisconsin
Madison, Wisconsin USA
July 30 - August 4, 2002


Name: Arndt, Karen M.
Mailing Address: Biological Sciences, University of Pittsburgh, 269 Crawford Hall, Pittsburgh, PA 15260, USA
Email Address: arndt@pitt.edu
Phone & FAX numbers: 412-624-6963 & 412-624-4759

Abstract #48


Session Title: Transcription, Elongation and Termination
Session Time: Friday, August 2 -- 11:00AM - 12:30PM
Presentation: Platform
Topic: Gene Expression

The Saccharomyces cerevisiae chromatin-modifying protein Chd1 interacts with the transcription elongation factors Rtf1 and Spt5.
Patrick J. Costa (1), Derek L. Lindstrom (2), Hien G. Tran (3), Kelli L. Roinick (1), Rajna Simic (1), Alexander D. Johnson (3), Grant A. Hartzog (2), Karen M. Arndt (1)
(1) Biological Sciences, University of Pittsburgh, 269 Crawford Hall, Pittsburgh, PA 15260, USA; (2) Department of MCD Biology, University of California, Santa Cruz, CA 95064; (3) Department of Biochemistry and Biophysics, University of California, San Francisco, CA 94143

Transcription elongation is an important regulatory step in gene expression. The product of the RTF1 gene interacts functionally and physically with proteins that regulate the elongation properties of RNA polymerase II. In addition, rtf1 mutations confer phenotypes often indicative of transcription elongation defects. We have recently shown that Rtf1 is a member of the RNA polymerase II-associated Paf1 complex and that this complex interacts with the conserved elongation factors Spt5-Spt4 and Spt16-Pob3. To further elucidate the function of Rtf1, we performed a two-hybrid screen for Rtf1-interacting proteins. We found that the chromatin-modifying protein Chd1 interacts with Rtf1 and that Chd1 levels are reduced in an rtf1 mutant strain, indicating the existence of a complex containing Rtf1 and Chd1. Our genetic results are in agreement with our biochemical studies. Most notably, in two genetic screens, we found that mutations in CHD1 can suppress the growth defect conferred by a pob3 mutation and the cold sensitivity caused by an spt5 mutation. The genetic interaction between Chd1 and Spt5 correlates with a physical interaction between these proteins. Together, these results suggest that a protein complex containing members of the Paf1 complex, Spt5-Spt4, Spt16-Pob3, and Chd1 regulates transcription elongation by RNA polymerase II. In support of this idea, we have recently found that Chd1, Rtf1, and Spt5 localize to the coding regions of actively transcribed genes.


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