MOT1-catalyzed TBP-DNA Disruption: Uncoupling DNA Conformational Change and Role of Upstream DNA

Overview

Journal EMBO J

Specialties Biotechnology
Molecular Biology

Date 2001 Apr 11

PMID 11296235

Citations 23

Authors

R P Darst

D Wang

D T Auble

Affiliations

Soon will be listed here.

Abstract

SNF2/SWI2-related ATPases employ ATP hydrolysis to disrupt protein-DNA interactions, but how ATP hydrolysis is coupled to disruption is not understood. Here we examine the mechanism of action of MOT1, a yeast SNF2/SWI2-related ATPase that uses ATP hydrolysis to remove TATA binding protein (TBP) from DNA. MOT1 function requires a 17 bp DNA 'handle' upstream of the TATA box, which must be double stranded. Remarkably, MOT1-catalyzed disruption of TBP-DNA does not appear to require DNA strand separation, DNA bending or twisting of the DNA helix. Thus, TBP-DNA disruption is accomplished in a reaction apparently not driven by a change in DNA structure. MOT1 action is supported by DNA templates in which the handle is connected to the TATA box via single-stranded DNA, indicating that the upstream duplex DNA can be conformationally uncoupled from the TATA box. Combining these results with proposed similarities between SNF2/SWI2 ATPases and helicases, we suggest that MOT1 uses ATP hydrolysis to translocate along the handle and thereby disrupt interactions between TBP and DNA.

Citing Articles

Structural basis for TBP displacement from TATA box DNA by the Swi2/Snf2 ATPase Mot1.

Woike S, Eustermann S, Jung J, Wenzl S, Hagemann G, Bartho J Nat Struct Mol Biol. 2023; 30(5):640-649.

PMID: 37106137 PMC: 7615866. DOI: 10.1038/s41594-023-00966-0.

Conformational changes and catalytic inefficiency associated with Mot1-mediated TBP-DNA dissociation.

Heiss G, Ploetz E, Voith von Voithenberg L, Viswanathan R, Glaser S, Schluesche P Nucleic Acids Res. 2019; 47(6):2793-2806.

PMID: 30649478 PMC: 6451094. DOI: 10.1093/nar/gky1322.

Crystal structure of the full Swi2/Snf2 remodeler Mot1 in the resting state.

Butryn A, Woike S, Shetty S, Auble D, Hopfner K Elife. 2018; 7.

PMID: 30289385 PMC: 6188472. DOI: 10.7554/eLife.37774.

Molecular Mechanism of Mot1, a TATA-binding Protein (TBP)-DNA Dissociating Enzyme.

Viswanathan R, True J, Auble D J Biol Chem. 2016; 291(30):15714-26.

PMID: 27255709 PMC: 4957054. DOI: 10.1074/jbc.M116.730366.

Structural basis for recognition and remodeling of the TBP:DNA:NC2 complex by Mot1.

Butryn A, Schuller J, Stoehr G, Runge-Wollmann P, Forster F, Auble D Elife. 2015; 4.

PMID: 26258880 PMC: 4565979. DOI: 10.7554/eLife.07432.

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