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Molecular and Cellular Biology, January 1999, p. 412-423, Vol. 19, No. 1
Department of Biochemistry and Molecular
Genetics, University of Virginia Health Science Center,
Charlottesville, Virginia 22908
Received 10 July 1998/Returned for modification 27 August
1998/Accepted 13 October 1998
Proteins in the SNF2/SWI2 family use ATP hydrolysis to catalyze
rearrangements in diverse protein-DNA complexes. How ATP hydrolysis is
coupled to these rearrangements is unknown, however. One attractive model is that these ATPases are ATP-dependent DNA-tracking enzymes. This idea was tested for the SNF2/SWI2 protein family member MOT1. MOT1
is an essential Saccharomyces cerevisiae transcription
factor that uses ATP to dissociate TATA binding protein (TBP) from DNA. By using a series of DNA templates with one or two TATA boxes in
combination with binding sites for heterologous DNA binding "roadblock" proteins, the ability of MOT1 to track along DNA was assayed. The results demonstrate that, following ATP-dependent TBP-DNA
dissociation, MOT1 dissociates rapidly from the DNA by a mechanism that
does not require a DNA end. Template commitment footprinting
experiments support the conclusion that ATP-dependent DNA tracking by
MOT1 does not occur. These results support a model in which MOT1 drives
TBP-DNA dissociation by a mechanism that involves a transient,
ATP-dependent interaction with TBP-DNA which does not involve
ATP-dependent DNA tracking.
0270-7306/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.
Testing for DNA Tracking by MOT1, a SNF2/SWI2
Protein Family Member
*
Corresponding author. Mailing address: Department of
Biochemistry and Molecular Genetics, University of Virginia Health
Science Center, Box 440, Charlottesville, VA 22908. Phone: (804)
243-2629. Fax: (804) 924-5069. E-mail: dta4n{at}virginia.edu.
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