Combined computational and experimental analysis of a complex of ribonuclease III and the regulatory macrodomain protein, YmdB.

ABSTRACT: Ribonuclease III is a conserved bacterial endonuclease that cleaves double-stranded(ds) structures in diverse coding and noncoding RNAs. RNase III is subject to multiple levels of control that in turn confer global post-transcriptional regulation. The Escherichia coli macrodomain protein YmdB directly interacts with RNase III, and an increase in YmdB amount in vivo correlates with a reduction in RNase III activity. Here, a computational-based structural analysis was performed to identify atomic-level features of the YmdB-RNase III interaction. The docking of monomeric E. coli YmdB with a homology model of the E. coli RNase III homodimer yields a complex that exhibits an interaction of the conserved YmdB residue R40 with specific RNase III residues at the subunit interface. Surface Plasmon

SUBMITTER: Paudyal S 

PROVIDER: S-EPMC4329070 | biostudies-literature | 2015 Mar

REPOSITORIES: biostudies-literature