Skip Navigation

Nucleic Acids Research 2005 33(16):5120-5132; doi:10.1093/nar/gki828
This Article
Right arrow Full Text Freely available
Right arrow Print PDF (2626K) Freely available
Right arrow Screen PDF (2070K) Freely available
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in ISI Web of Science
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Search for citing articles in:
ISI Web of Science (11)
Right arrow Commercial Re-use Guidelines
for Open Access NAR Content
Google Scholar
Right arrow Articles by Sharin, E.
Right arrow Articles by Jarrous, N.
Right arrow Search for Related Content
PubMed
Right arrow Articles by Sharin, E.
Right arrow Articles by Jarrous, N.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Published online 9 September 2005

© The Author 2005. Published by Oxford University Press. All rights reserved
The online version of this article has been published under an open access model. Users are entitled to use, reproduce, disseminate, or display the open access version of this article for non-commercial purposes provided that: the original authorship is properly and fully attributed; the Journal and Oxford University Press are attributed as the original place of publication with the correct citation details given; if an article is subsequently reproduced or disseminated not in its entirety but only in part or as a derivative work this must be clearly indicated. For commercial re-use, please contact journals.permissions{at}oxfordjournals.org

Article

RNase P: role of distinct protein cofactors in tRNA substrate recognition and RNA-based catalysis

Ela Sharin, Aleks Schein, Hagit Mann, Yitzhak Ben-Asouli and Nayef Jarrous*

Department of Molecular Biology, The Hebrew University-Hadassah Medical School Jerusalem 91120, Israel

*To whom correspondence should be addressed. Tel: +972 2 6758233; Fax: +972 2 6784010; Email: jarrous{at}md.huji.ac.il

Received January 24, 2005. Revised May 22, 2005. Accepted August 24, 2005.

The Escherichia coli ribonuclease P (RNase P) has a protein component, termed C5, which acts as a cofactor for the catalytic M1 RNA subunit that processes the 5' leader sequence of precursor tRNA. Rpp29, a conserved protein subunit of human RNase P, can substitute for C5 protein in reconstitution assays of M1 RNA activity. To better understand the role of the former protein, we compare the mode of action of Rpp29 to that of the C5 protein in activation of M1 RNA. Enzyme kinetic analyses reveal that complexes of M1 RNA–Rpp29 and M1 RNA–C5 exhibit comparable binding affinities to precursor tRNA but different catalytic efficiencies. High concentrations of substrate impede the activity of the former complex. Rpp29 itself exhibits high affinity in substrate binding, which seems to reduce the catalytic efficiency of the reconstituted ribonucleoprotein. Rpp29 has a conserved C-terminal domain with an Sm-like fold that mediates interaction with M1 RNA and precursor tRNA and can activate M1 RNA. The results suggest that distinct protein folds in two unrelated protein cofactors can facilitate transition from RNA- to ribonucleoprotein-based catalysis by RNase P.

The authors wish it to be known that, in their opinion, the first two authors should be regarded as joint First Authors


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
 Nucleic Acids ResHome page
T. V. Aspinall, J. M.B. Gordon, H. J. Bennett, P. Karahalios, J.-P. Bukowski, S. C. Walker, D. R. Engelke, and J. M. Avis
Interactions between subunits of Saccharomyces cerevisiae RNase MRP support a conserved eukaryotic RNase P/MRP architecture
Nucleic Acids Res., October 8, 2007; 35(19): 6439 - 6450.
[Abstract] [Full Text] [PDF]

Home page
 Nucleic Acids ResHome page
N. Jarrous and R. Reiner
Human RNase P: a tRNA-processing enzyme and transcription factor
Nucleic Acids Res., June 28, 2007; 35(11): 3519 - 3524.
[Abstract] [Full Text] [PDF]

Home page
 J. Bacteriol.Home page
M. Gossringer, R. Kretschmer-Kazemi Far, and R. K. Hartmann
Analysis of RNase P Protein (rnpA) Expression in Bacillus subtilis Utilizing Strains with Suppressible rnpA Expression.
J. Bacteriol., October 1, 2006; 188(19): 6816 - 6823.
[Abstract] [Full Text] [PDF]

Home page
 J BiochemHome page
A. Terada, T. Honda, H. Fukuhara, K. Hada, and M. Kimura
Characterization of the Archaeal Ribonuclease P Proteins from Pyrococcus horikoshii OT3
J. Biochem., August 1, 2006; 140(2): 293 - 298.
[Abstract] [Full Text] [PDF]

Home page
 RNAHome page
T. J.M. Welting, B. J. Kikkert, W. J. van Venrooij, and G. J.M. Pruijn
Differential association of protein subunits with the human RNase MRP and RNase P complexes
RNA, July 1, 2006; 12(7): 1373 - 1382.
[Abstract] [Full Text] [PDF]


Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.