title: The catalytic core of RNase P.
abstract: A deletion mutant of the catalytic RNA component of Escherichia coli RNase P missing residues 87-241 retains the ability to interact with the protein component to form a functional catalyst. The deletion of this phylogenetically conserved region significantly increases the Km, indicating that the deleted structures may be important for binding to the precursor tRNA substrate but not for the cleavage reaction. Under some reaction conditions, this RNase P deletion mutant can become a relatively non-specific nuclease, indicating that this RNA's catalytic center may be more exposed. The catalytic core of the RNase P is formed by less than one third of the 377 residues of the RNase P RNA.
authors.affiliation: SRI International, Menlo Park, CA 94025-3493, USA.
authors.forename: C J
authors.initials: CJ
authors.lastname: Green
authors.forename: R
authors.initials: R
authors.lastname: Rivera-León
authors.forename: B S
authors.initials: BS
authors.lastname: Vold
mesh_terms: D001412:Bacillus subtilis / Q000378:metabolism; D001483:Base Sequence; D001665:Binding Sites; D002384:Catalysis; D003001:Cloning, Molecular; D004722:Endoribonucleases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D004926:Escherichia coli / Q000201:enzymology*; D029968:Escherichia coli Proteins; D008969:Molecular Sequence Data; D009690:Nucleic Acid Conformation; D012329:RNA, Bacterial / Q000737:chemistry / Q000378:metabolism; D016337:RNA, Catalytic / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D012346:RNA, Transfer, Amino Acyl / Q000378:metabolism; D043262:Ribonuclease P; D017384:Sequence Deletion; D013329:Structure-Activity Relationship; D013379:Substrate Specificity
chemical_list: D029968:Escherichia coli Proteins; D012329:RNA, Bacterial; D016337:RNA, Catalytic; D012346:RNA, Transfer, Amino Acyl; D004722:Endoribonucleases; D043262:Ribonuclease P; C470865:ribonuclease P, E coli