AI Article Synopsis
- - Swi2/Snf2 ATPases are important for remodeling nucleosomes and transcription complexes, but there is limited structural information about their mechanisms of action.
- - The study focuses on the Mot1 protein, which disrupts TATA box-binding protein (TBP):DNA complexes, to explore the structural mechanisms of these ATPases.
- - Researchers determined the crystal structure of Mot1's N-terminal domain with TBP, DNA, and an associated regulator (NC2), revealing how Mot1 modifies DNA and influences protein interactions without ATP.
Article Abstract
Swi2/Snf2 ATPases remodel substrates such as nucleosomes and transcription complexes to control a wide range of DNA-associated processes, but detailed structural information on the ATP-dependent remodeling reactions is largely absent. The single subunit remodeler Mot1 (modifier of transcription 1) dissociates TATA box-binding protein (TBP):DNA complexes, offering a useful system to address the structural mechanisms of Swi2/Snf2 ATPases. Here, we report the crystal structure of the N-terminal domain of Mot1 in complex with TBP, DNA, and the transcription regulator negative cofactor 2 (NC2). Our data show that Mot1 reduces DNA:NC2 interactions and unbends DNA as compared to the TBP:DNA:NC2 state, suggesting that Mot1 primes TBP:NC2 displacement in an ATP-independent manner. Electron microscopy and cross-linking data suggest that the Swi2/Snf2 domain of Mot1 associates with the upstream DNA and the histone fold of NC2, thereby revealing parallels to some nucleosome remodelers. This study provides a structural framework for how a Swi2/Snf2 ATPase interacts with its substrate DNA:protein complex.
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4565979 | PMC |
| http://dx.doi.org/10.7554/eLife.07432 | DOI Listing |
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