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Originally published as Genetics Published Articles Ahead of Print on April 30, 2006.
Genetics, Vol. 173, 1871-1884, August 2006, Copyright © 2006
doi:10.1534/genetics.106.058834
Genetic Interactions Between TFIIF and TFIIS
Rachel N. Fish*,
Michelle L. Ammerman
,
Judith K. Davie*,1,
Betty F. Lu*,
Cindy Pham*,
LeAnn Howe
,
Alfred S. Ponticelli and
Caroline M. Kane*,2
* Department of Molecular and Cell Biology, University of California, Berkeley, CA 94720-3202, Department of Biochemistry, School of Medicine and Biomedical Sciences, SUNY, Buffalo, NY 14214-3000 and Department of Biochemistry and Molecular Biology, University of British Columbia, Vancouver, British Columbia V5Z 4H4, Canada
2 Corresponding author: Department of Molecular and Cell Biology, 408 Barker Hall, University of California, Berkeley, CA 94720-3202.
E-mail: kanecm{at}berkeley.edu
The eukaryotic transcript elongation factor TFIIS is encoded by a nonessential gene, PPR2, in Saccharomyces cerevisiae. Disruptions of PPR2 are lethal in conjunction with a disruption in the nonessential gene TAF14/TFG3. While investigating which of the Taf14p-containing complexes may be responsible for the synthetic lethality between ppr2
and taf14, we discovered genetic interactions between PPR2 and both TFG1 and TFG2 encoding the two larger subunits of the TFIIF complex that also contains Taf14p. Mutant alleles of tfg1 or tfg2 that render cells cold sensitive have improved growth at low temperature in the absence of TFIIS. Remarkably, the amino-terminal 130 amino acids of TFIIS, which are dispensable for the known in vitro and in vivo activities of TFIIS, are required to complement the lethality in taf14 ppr2 cells. Analyses of deletion and chimeric gene constructs of PPR2 implicate contributions by different regions of this N-terminal domain. No strong common phenotypes were identified for the ppr2 and taf14 strains, implying that the proteins are not functionally redundant. Instead, the absence of Taf14p in the cell appears to create a dependence on an undefined function of TFIIS mediated by its N-terminal region. This region of TFIIS is also at least in part responsible for the deleterious effect of TFIIS on tfg1 or tfg2 cold-sensitive cells. Together, these results suggest a physiologically relevant functional connection between TFIIS and TFIIF.
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