The recognition of structured elements by a conserved groove distant from domains associated with catalysis is an essential determinant of RNase E.

ABSTRACT: RNase E is an endoribonuclease found in many bacteria, including important human pathogens. Within Escherichia coli, it has been shown to have a major role in both the maturation of all classes of RNA involved in translation and the initiation of mRNA degradation. Thus, knowledge of the major determinants of RNase E cleavage is central to our understanding and manipulation of bacterial gene expression. We show here that the binding of RNase E to structured RNA elements is crucial for the processing of tRNA, can activate catalysis and may be important in mRNA degradation. The recognition of structured elements by RNase E is mediated by a recently discovered groove that is distant from the domains associated with catalysis. The functioning of this groove is shown here to be essential for E.

SUBMITTER: Clarke JE 

PROVIDER: S-EPMC9841416 | biostudies-literature | 2023 Jan

REPOSITORIES: biostudies-literature