Nucleic Acids Research, 1995, Vol. 23, No. 5 767-772
© 1995
MOLECULAR BIOLOGY |
An interaction between the Tfb1 and SsI1 subunits of yeast TFIIH correlates with DNA repair activity
Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School 240 Longwood Avenue, Boston, MA 02115, USA
*To whom correspondence should be addressed
Received November 18, 1994. Accepted January 20, 1995.
Yeast transcription factor TFIIH (also known as factor b) is a component of the RNA polymerase II Initiation complex. Several TFIIH subunits (RAD3, SSL2 and SSL1) have also been implicated in DNA repair. Ssl1 interacts directly with another TFIIH subunlt, Tfb1, which has not previously been shown to have a role in DNA repair. We isolated mutations in TFB1 that lead to a temperature sensitive phenotype. These mutations result in C-terminal truncations of the Tfb1 protein and disrupt its interaction with Ssl1. The C-terminal 114 amino acids of Tfb1 arenecessary and sufficient for this interaction. Interestingly, cells carrying these truncations In Tfb1 cause sensitivity to ultraviolet (UV) light induced DNA damage, as previously observed for mutations in RAD3, SSL1 and SSL2. Many other mutations in RNA polymerase II basal factors were tested and found not to cause an increase in UV sensitivity, indicating that this phenotype is not due to a general defect in transcription.
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