The phage T4 MotA transcription factor contains a novel DNA binding motif that specifically recognizes modified DNA.

ABSTRACT: During infection, bacteriophage T4 produces the MotA transcription factor that redirects the host RNA polymerase to the expression of T4 middle genes. The C-terminal 'double-wing' domain of MotA binds specifically to the MotA box motif of middle T4 promoters. We report the crystal structure of this complex, which reveals a new mode of protein-DNA interaction. The domain binds DNA mostly via interactions with the DNA backbone, but the binding is enhanced in the specific cognate structure by additional interactions with the MotA box motif in both the major and minor grooves. The linker connecting the two MotA domains plays a key role in stabilizing the complex via minor groove interactions. The structure is consistent with our previous model derived from chemical cleavage experiments using t

SUBMITTER: Cuypers MG 

PROVIDER: S-EPMC6007404 | biostudies-literature | 2018 Jun

REPOSITORIES: biostudies-literature