Differential role of the intermolecular base-pairs G292-C 75 and G293-C 74 in the reaction catalyzed by Escherichia coli RNase P RNA 1 1Edited by A. R. Fersht
- 1 June 2000
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 299 (4) , 941-951
- https://doi.org/10.1006/jmbi.2000.3789
Abstract
No abstract availableKeywords
This publication has 31 references indexed in Scilit:
- RNase P RNA structure and cleavage reflect the primary structure of tRNA genes 1 1Edited by J. KarnJournal of Molecular Biology, 1998
- RNase P from a Photosynthetic Organelle Contains an RNA Homologous to the Cyanobacterial CounterpartJournal of Molecular Biology, 1996
- Kinetics and Thermodynamics of the RNase P RNA Cleavage Reaction:Analysis of tRNA 3'-end VariantsJournal of Molecular Biology, 1995
- A Kinetic Mechanism for Cleavage of Precursor tRNAAsp Catalyzed by the RNA Component of Bacillus subtilis Ribonuclease PBiochemistry, 1994
- Lead‐ion‐induced cleavage of RNase P RNAEuropean Journal of Biochemistry, 1994
- Gel retardation analysis ofE.coliM1 RNA-tRNA complexesNucleic Acids Research, 1993
- Improved free-energy parameters for predictions of RNA duplex stability.Proceedings of the National Academy of Sciences, 1986
- Hydrogen bonding and biological specificity analysed by protein engineeringNature, 1985
- The RNA moiety of ribonuclease P is the catalytic subunit of the enzymePublished by Elsevier ,1983
- 3'-Phosphatase activity in T4 polynucleotide kinaseBiochemistry, 1977