Skip Navigation

Nucleic Acids Research 2004 32(12):3703-3711; doi:10.1093/nar/gkh689
This Article
Right arrow Full Text Freely available
Right arrow Print PDF (420K) 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 Similar articles in PubMed
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 (9)
Right arrow Commercial Re-use Guidelines
for Open Access NAR Content
Google Scholar
Right arrow Articles by Li, X.
Right arrow Articles by Lindahl, L.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Li, X.
Right arrow Articles by Lindahl, L.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Published online 14 July 2004

Nucleic Acids Research, Vol. 32 No. 12 © Oxford University Press 2004; all rights reserved

Identification of a functional core in the RNA component of RNase MRP of budding yeasts

Xing Li, Sephorah Zaman, Yvette Langdon, Janice M. Zengel and Lasse Lindahl*

Department of Biological Sciences, UMBC, 1000 Hilltop Circle, Baltimore, MD 21250, USA

* To whom correspondence should be addressed. Tel: +1 410 455 2996; Fax: +1 410 455 3875; Email: Lindahl{at}umbc.edu

Received February 16, 2004; Revised May 25, 2004; Accepted June 18, 2004

RNase MRP is an endonuclease participating in ribosomal RNA processing. It consists of one RNA and at least nine protein subunits. Using oligonucleotide-directed mutagenesis, we analyzed the functional role of five of the hairpins in the secondary structure of the RNA subunit of Saccharomyces cerevisiae RNase MRP. Deletion of an entire hairpin was either lethal or resulted in very poor growth. However, peripheral portions constituting up to 70% of a hairpin could be deleted without effects on cell growth rate or processing of rRNA. To determine whether these hairpins perform redundant functions, we analyzed mutants combining four or five benign hairpin deletions. Simultaneous removal of four of these hairpin segments had no detectable effect. Removing five created a temperature- and cold-sensitive enzyme, but these deficiencies could be partially overcome by a mutation in one of the RNase MRP protein subunits, or by increasing the copy number of several of the protein subunit genes. These observations suggest that the peripheral elements of the RNA hairpins contain no structures or sequences required for substrate recognition, catalysis or binding of protein subunits. Thus, the functionally essential elements of the RNase MRP RNA appear to be concentrated in the core of the subunit.


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
 RNAHome page
K. Chakrabarti, M. Pearson, L. Grate, T. Sterne-Weiler, J. Deans, J. P. Donohue, and M. Ares Jr
Structural RNAs of known and unknown function identified in malaria parasites by comparative genomics and RNA analysis
RNA, November 1, 2007; 13(11): 1923 - 1939.
[Abstract] [Full Text] [PDF]

Home page
 RNAHome page
T. J.M. Welting, F. M.A. Peters, S. M.M. Hensen, N. L. van Doorn, B. J. Kikkert, J. M.H. Raats, W. J. van Venrooij, and G. J.M. Pruijn
Heterodimerization regulates RNase MRP/RNase P association, localization, and expression of Rpp20 and Rpp25
RNA, January 1, 2007; 13(1): 65 - 75.
[Abstract] [Full Text] [PDF]

Home page
 RNAHome page
S. Xiao, J. Hsieh, R. L. Nugent, D. J. Coughlin, C. A. Fierke, and D. R. Engelke
Functional characterization of the conserved amino acids in Pop1p, the largest common protein subunit of yeast RNases P and MRP
RNA, June 1, 2006; 12(6): 1023 - 1037.
[Abstract] [Full Text] [PDF]

Home page
 RNAHome page
Y. Zhu, V. Stribinskis, K. S. Ramos, and Y. Li
Sequence analysis of RNase MRP RNA reveals its origination from eukaryotic RNase P RNA
RNA, May 1, 2006; 12(5): 699 - 706.
[Abstract] [Full Text] [PDF]

Home page
 Nucleic Acids ResHome page
P. Piccinelli, M. A. Rosenblad, and T. Samuelsson
Identification and analysis of ribonuclease P and MRP RNA in a broad range of eukaryotes
Nucleic Acids Res., August 8, 2005; 33(14): 4485 - 4495.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
K. Salinas, S. Wierzbicki, L. Zhou, and M. E. Schmitt
Characterization and Purification of Saccharomyces cerevisiae RNase MRP Reveals a New Unique Protein Component
J. Biol. Chem., March 25, 2005; 280(12): 11352 - 11360.
[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.