Logo Logo
Switch Language to German
Butryn, Agata; Schuller, Jan M.; Stoehr, Gabriele; Runge-Wollmann, Petra; Förster, Friedrich; Auble, David T.; Hopfner, Karl-Peter (2015): Structural basis for recognition and remodeling of the TBP:DNA:NC2 complex by Mot1. In: eLife, Vol. 4, e07432


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.