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

摘要: 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 1) dissociates TATA box-binding protein (TBP):DNA complexes, offering useful system address mechanisms ATPases. Here, we report crystal structure N-terminal domain in complex with TBP, DNA, regulator negative cofactor 2 (NC2). Our data show that reduces DNA:NC2 interactions unbends DNA compared TBP:DNA:NC2 state, suggesting primes TBP:NC2 displacement an ATP-independent manner. Electron microscopy cross-linking suggest associates upstream histone fold NC2, thereby revealing parallels some nucleosome remodelers. This study provides framework for how ATPase interacts its substrate DNA:protein complex.