Skip Navigation

This Article
Right arrow Full Text Freely available
Right arrow Print PDF (354K) 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 (14)
Right arrowRequest Permissions
Right arrow Commercial Re-use Guidelines
for Open Access NAR Content
Google Scholar
Right arrow Articles by Walsh, A. P.
Right arrow Articles by McDowall, K. J.
Right arrow Search for Related Content
PubMed
Right arrow Articles by Walsh, A. P.
Right arrow Articles by McDowall, K. J.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Nucleic Acids Research, 2001, Vol. 29, No. 9 1864-1871
© 2001 Oxford University Press

Cleavage of poly(A) tails on the 3'-end of RNA by ribonuclease E of Escherichia coli

A. P. Walsh, M. R. Tock, M. H. Mallen, V. R. Kaberdin1, A. von Gabain1 and K. J. McDowall*

Astbury Centre for Structural Molecular Biology, Faculty of Biological Sciences, University of Leeds, Leeds LS2 9JT, UK and 1Institute of Microbiology and Genetics, Vienna Biocenter, A-1030 Vienna, Austria

RNase E initiates the decay of Escherichia coli RNAs by cutting them internally near their 5'-end and is a component of the RNA degradosome complex, which also contains the 3'-exonuclease PNPase. Recently, RNase E has been shown to be able to remove poly(A) tails by what has been described as an exonucleolytic process that can be blocked by the presence of a phosphate group on the 3'-end of the RNA. We show here, however, that poly(A) tail removal by RNase E is in fact an endonucleolytic process that is regulated by the phosphorylation status at the 5'- but not the 3'-end of RNA. The rate of poly(A) tail removal by RNase E was found to be 30-fold greater when the 5'-terminus of RNA substrates was converted from a triphosphate to monophosphate group. This finding prompted us to re-analyse the contributions of the ribonucleolytic activities within the degradosome to 3' attack since previous studies had only used substrates that had a triphosphate group on their 5'-end. Our results indicate that RNase E associated with the degradosome may contribute to the removal of poly(A) tails from 5'-monophosphorylated RNAs, but this is only likely to be significant should their attack by PNPase be blocked.

* To whom correspondence should be addressed. Tel: +44 113 233 3109; Fax: +44 113 233 1407; Email: k.j.mcdowall{at}leeds.ac.uk Present addresses:  A. P. Walsh, MRC Laboratory of Molecular Biology, Cambridge CB2 2QH, UKM. R. Tock, Department of Chemistry, University of Sheffield, Sheffield S3 7HF, UK 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
K. Y. Song, C. K. Hwang, C. S. Kim, H. S. Choi, P.-Y. Law, L.-N. Wei, and H. H. Loh
Translational repression of mouse mu opioid receptor expression via leaky scanning
Nucleic Acids Res., March 12, 2007; 35(5): 1501 - 1513.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
J. M. Caruthers, Y. Feng, D. B. McKay, and S. N. Cohen
Retention of Core Catalytic Functions by a Conserved Minimal Ribonuclease E Peptide That Lacks the Domain Required for Tetramer Formation
J. Biol. Chem., September 15, 2006; 281(37): 27046 - 27051.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
Y. Redko, M. R. Tock, C. J. Adams, V. R. Kaberdin, J. A. Grasby, and K. J. McDowall
Determination of the Catalytic Parameters of the N-terminal Half of Escherichia coli Ribonuclease E and the Identification of Critical Functional Groups in RNA Substrates
J. Biol. Chem., November 7, 2003; 278(45): 44001 - 44008.
[Abstract] [Full Text] [PDF]

Home page
 Nucleic Acids ResHome page
V. R. Kaberdin
Probing the substrate specificity of Escherichia coli RNase E using a novel oligonucleotide-based assay
Nucleic Acids Res., August 15, 2003; 31(16): 4710 - 4716.
[Abstract] [Full Text] [PDF]

Home page
 Nucleic Acids ResHome page
J. Le Derout, M. Folichon, F. Briani, G. Deho, P. Regnier, and E. Hajnsdorf
Hfq affects the length and the frequency of short oligo(A) tails at the 3' end of Escherichia coli rpsO mRNAs
Nucleic Acids Res., July 15, 2003; 31(14): 4017 - 4023.
[Abstract] [Full Text] [PDF]

Home page
 Proc. Natl. Acad. Sci. USAHome page
Y. Feng, T. A. Vickers, and S. N. Cohen
The catalytic domain of RNase E shows inherent 3' to 5' directionality in cleavage site selection
PNAS, November 12, 2002; 99(23): 14746 - 14751.
[Abstract] [Full Text] [PDF]

Home page
 J. Bacteriol.Home page
S. R. Kushner
mRNA Decay in Escherichia coli Comes of Age
J. Bacteriol., September 1, 2002; 184(17): 4658 - 4665.
[Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
A. Hicks, R. G. Drager, D. C. Higgs, and D. B. Stern
An mRNA 3' Processing Site Targets Downstream Sequences for Rapid Degradation in Chlamydomonas Chloroplasts
J. Biol. Chem., January 25, 2002; 277(5): 3325 - 3333.
[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.