Small-angle x-ray and neutron scattering of MexR and its complex with DNA supports a conformational selection binding model.

ABSTRACT: In this work, we used small-angle x-ray and neutron scattering to reveal the shape of the protein-DNA complex of the Pseudomonas aeruginosa transcriptional regulator MexR, a member of the multiple antibiotics resistance regulator (MarR) family, when bound to one of its native DNA binding sites. Several MarR-like proteins, including MexR, repress the expression of efflux pump proteins by binding to DNA on regulatory sites overlapping with promoter regions. When expressed, efflux proteins self-assemble to form multiprotein complexes and actively expel highly toxic compounds out of the host organism. The mutational pressure on efflux-regulating MarR family proteins is high since deficient DNA binding leads to constitutive expression of efflux pumps and thereby supports acquired multidrug resi

SUBMITTER: Caporaletti F 

PROVIDER: S-EPMC9892617 | biostudies-literature | 2023 Jan

REPOSITORIES: biostudies-literature