Article
- The EMBO Journal (2003) 22, 3131 - 3141
- doi:10.1093/emboj/cdg304
Subject Category:
High-affinity DNA binding by a Mot1p–TBP complex: implications for TAF-independent transcription
Orlando H. Gumbs1, Allyson M. Campbell2 and P.Anthony Weil1
- Department of Molecular Physiology and Biophysics, Vanderbilt University, School of Medicine, Nashville, TN 37232-0615, USA
- Present address: Department of Medicine, Stanford University, Palo Alto, CA 94305, USA
Correspondence to:
P.Anthony Weil, E-mail: tony.weil@vanderbilt.edu
Received 31 October 2002; Accepted 28 April 2003; Revised 15 April 2003
Abstract
Yeast Mot1p, an abundant conserved member of the Snf2p-ATPase family of proteins, both dissociates TBP from DNA in vitro using the energy of ATP and represses gene transcription in vivo, yet paradoxically, loss of Mot1p function also leads to decreased transcription of certain genes. We conducted experiments utilizing fluorescently labeled DNA, TBP, fluorescence anisotropy spectroscopy and native gel electrophoresis to study Mot1p action. We have made a number of observations, the most intriguing being that a stable Mot1p–TBP complex has the ability to bind TATA DNA with high affinity, albeit with dramatically altered specificity. We propose that this altered TBP–DNA recognition is integral to Mot1p's ability to regulate transcription, and further postulate that the Mot1p–TBP complex delivers TBP to TAF-independent mRNA encoding genes.
Keywords:
- ATPase/DNA binding/Mot1p/TBP/transcription regulation
