The DNA Recognition Motif of GapR Has an Intrinsic DNA Binding Preference towards AT-rich DNA.

ABSTRACT: The nucleoid-associated protein GapR found in Caulobacter crescentus is crucial for DNA replication, transcription, and cell division. Associated with overtwisted DNA in front of replication forks and the 3' end of highly-expressed genes, GapR can stimulate gyrase and topo IV to relax (+) supercoils, thus facilitating the movement of the replication and transcription machines. GapR forms a dimer-of-dimers structure in solution that can exist in either an open or a closed conformation. It initially binds DNA through the open conformation and then undergoes structural rearrangement to form a closed tetramer, with DNA wrapped in the central channel. Here, we show that the DNA binding domain of GapR (residues 1-72, GapR^ΔC17) exists as a dimer in solution and adopts the

SUBMITTER: Huang Q 

PROVIDER: S-EPMC8510090 | biostudies-literature | 2021 Sep

REPOSITORIES: biostudies-literature