A structural and biochemical comparison of Ribonuclease E homologues from pathogenic bacteria highlights species-specific properties.

ABSTRACT: Regulation of gene expression through processing and turnover of RNA is a key mechanism that allows bacteria to rapidly adapt to changing environmental conditions. Consequently, RNA degrading enzymes (ribonucleases; RNases) such as the endoribonuclease RNase E, frequently play critical roles in pathogenic bacterial virulence and are potential antibacterial targets. RNase E consists of a highly conserved catalytic domain and a variable non-catalytic domain that functions as the structural scaffold for the multienzyme degradosome complex. Despite conservation of the catalytic domain, a recent study identified differences in the response of RNase E homologues from different species to the same inhibitory compound(s). While RNase E from Escherichia coli has been well-characterised, far less is

SUBMITTER: Mardle CE 

PROVIDER: S-EPMC6538622 | biostudies-literature | 2019 May

REPOSITORIES: biostudies-literature