Home

About

Advanced Search

Browse by Discipline

Scientific Societies

E-print Alerts

Add E-prints

E-print Network
FAQHELPSITE MAPCONTACT US


  Advanced Search  

 
MOLECULAR AND CELLULAR BIOLOGY, 0270-7306/99/$04.00 0
 

Summary: MOLECULAR AND CELLULAR BIOLOGY,
0270-7306/99/$04.00 0
Jan. 1999, p. 412423 Vol. 19, No. 1
Copyright 1999, American Society for Microbiology. All Rights Reserved.
Testing for DNA Tracking by MOT1, a SNF2/SWI2 Protein
Family Member
DAVID T. AUBLE* AND SUSANNE M. STEGGERDA
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

  

Source: Auble, David - Department of Biochemistry and Molecular Genetics, University of Virginia

 

Collections: Biology and Medicine