DNA binding induces a cis-to-trans switch in Cre recombinase to enable intasome assembly.

ABSTRACT: Mechanistic understanding of DNA recombination in the Cre-loxP system has largely been guided by crystallographic structures of tetrameric synaptic complexes. Those studies have suggested a role for protein conformational dynamics that has not been well characterized at the atomic level. We used solution nuclear magnetic resonance (NMR) spectroscopy to discover the link between intrinsic flexibility and function in Cre recombinase. Transverse relaxation-optimized spectroscopy (TROSY) NMR spectra show the N-terminal and C-terminal catalytic domains (Cre^NTD and Cre^Cat) to be structurally independent. Amide ¹⁵N relaxation measurements of the Cre^Cat domain reveal fast-timescale dynamics in most regions that exhibit conformational differences i

SUBMITTER: Unnikrishnan A 

PROVIDER: S-EPMC7547242 | biostudies-literature | 2020 Oct

REPOSITORIES: biostudies-literature