HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Gardiner, K. Articles by Pace, N. R. Search for Related Content PubMed PubMed Citation Articles by Gardiner, K. Articles by Pace, N. R. Social Bookmarking                      What's this?

J. Biol. Chem., Vol. 255, Issue 16, 7507-7509, 08, 1980

RNase P of Bacillus subtilis has a RNA component

K Gardiner and NR Pace

Ribonuclease P from Bacillus subtilis cleaves a Gln-Leu tRNA dimeric precursor from bacteriophage T4-infected Escherichia coli, yielding products identical with those generated by the E. coli RNase P. Using this tRNA dimer as an assay substrate, the RNase of P of B. subtilis was shown to consist of at least two components, one of which bands in CsCl equilibrium buoyant density centrifugation at 1.7 g/ml, characteristic of a protein x nucleic acid complex. Both this component and a second, retrieved from the low density (less than 1.4 g/ml) regions of CsCl gradients, are required for RNase P activity. Enzyme activity is abolished by treating the component of density 1.7 g/ml with insoluble RNase A prior to assay. These observations suggest that the RNase P of B. subtilis, like that of E. coli, contain a RNA component essential for activity. That this RNA component is of functional importance, and not an artifact of isolation procedures, is supported by the fact that it is observed in these two phylogenetically disparate organisms.
CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				S. Yao, J. B. Blaustein, and D. H. Bechhofer Processing of Bacillus subtilis small cytoplasmic RNA: evidence for an additional endonuclease cleavage site Nucleic Acids Res., July 26, 2007; 35(13): 4464 - 4473. [Abstract] [Full Text] [PDF]

				E. Seif, A. Cadieux, and B. F. Lang Hybrid E. coli--Mitochondrial ribonuclease P RNAs are catalytically active RNA, September 1, 2006; 12(9): 1661 - 1670. [Abstract] [Full Text] [PDF]

				K. Li and R. S. Williams Cloning and Characterization of Three New Murine Genes Encoding Short Homologues of RNase P RNA J. Biol. Chem., October 20, 1995; 270(42): 25281 - 25285. [Abstract] [Full Text] [PDF]

				D. Waugh, C. Green, and N. Pace The design and catalytic properties of a simplified ribonuclease P RNA Science, June 30, 1989; 244(4912): 1569 - 1571. [Abstract] [PDF]

				C Reich, G. Olsen, B Pace, and N. Pace Role of the protein moiety of ribonuclease P, a ribonucleoprotein enzyme Science, January 8, 1988; 239(4836): 178 - 181. [Abstract] [PDF]

				D. Chang and D. Clayton A mammalian mitochondrial RNA processing activity contains nucleus-encoded RNA Science, March 6, 1987; 235(4793): 1178 - 1184. [Abstract] [PDF]

				A. Zaug, Kent JR, and T. Cech A labile phosphodiester bond at the ligation junction in a circular intervening sequence RNA Science, May 11, 1984; 224(4649): 574 - 578. [Abstract] [PDF]