The Catalytic Core of RNase P

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 de...

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Bibliographic Details
Published in:Nucleic acids research 1996-04, Vol.24 (8), p.1497-1503
Main Authors: Green, Christopher J., Rivera-León, Rafael, Void, Barbara S.
Format: Article
Language:English
Subjects:
Bacillus subtilis - metabolism
Base Sequence
Binding Sites
Catalysis
Cloning, Molecular
Endoribonucleases - chemistry
Endoribonucleases - genetics
Endoribonucleases - metabolism
Escherichia coli
Escherichia coli - enzymology
Escherichia coli Proteins
Molecular Sequence Data
Nucleic Acid Conformation
Ribonuclease P
RNA, Bacterial - chemistry
RNA, Bacterial - metabolism
RNA, Catalytic - chemistry
RNA, Catalytic - genetics
RNA, Catalytic - metabolism
RNA, Transfer, Amino Acyl - metabolism
Sequence Deletion
Structure-Activity Relationship
Substrate Specificity
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Description
Summary: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.
ISSN:0305-1048
1362-4962
1362-4962
DOI:10.1093/nar/24.8.1497