title: RNase E: still a wonderfully mysterious enzyme.
abstract: Ribonuclease E (RNase E), which is encoded by an essential Escherichia coli gene known variously as rne, ams, and hmp, was discovered initially as an rRNA-processing enzyme but it is now known to have a general role in RNA decay. Multiple functions, including the ability to cleave RNA endonucleolytically in AU-rich single-strand regions, RNA-binding capabilities, and the ability to interact with polynucleotide phosphorylase and other proteins implicated in the processing and degradation of RNA, are encoded by its 1,061 amino acid residues. The presence of homologues and functional analogues of the rne gene in a variety of prokaryotic and eukaryotic species suggests that its functions have been highly conserved during evolution. While much has been learned in recent years about the structure and functions of RNase E, there is continuing mystery about possible additional activities and molecular interactions of this enzyme.
authors.affiliation: Department of Genetics, Stanford University, School of Medicine, California 94305-5120, USA. sncohen@forsythe.stanford.edu
authors.forename: S N
authors.initials: SN
authors.lastname: Cohen
authors.forename: K J
authors.initials: KJ
authors.lastname: McDowall
mesh_terms: D004722:Endoribonucleases / Q000235:genetics* / Q000502:physiology; D004926:Escherichia coli / Q000201:enzymology* / Q000235:genetics; D005798:Genes, Bacterial / Q000502:physiology*
chemical_list: D004722:Endoribonucleases; C022537:ribonuclease E