Nucleic Acids Research Advance Access originally published online on March 29, 2007
Nucleic Acids Research 2007 35(8):2494-2502; doi:10.1093/nar/gkm120
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Nucleic Acids Research, 2007, Vol. 35, No. 8 2494-2502
© 2007 The Author(s)
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.
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Polyadenylation of a functional mRNA controls gene expression in Escherichia coli
1Régulation de l’Expression Génétique chez les Microorganismes, UPR CNRS n° 9073, conventionnée avec l’Université Paris 7—Denis Diderot, Paris, France and 2Neurobiologie et Diversité Cellulaire, UMR CNRS n° 7637, Paris, France
*To whom correspondence should be addressed. Tel: +33 1 58 41 51 26; Fax: +33 1 58 41 50 20; Email: Eliane.Hajnsdorf{at}ibpc.fr
Received December 14, 2006. Revised February 12, 2007. Accepted February 12, 2007.
Although usually implicated in the stabilization of mRNAs in eukaryotes, polyadenylation was initially shown to destabilize RNA in bacteria. All the data are consistent with polyadenylation being part of a quality control process targeting folded RNA fragments and non-functional RNA molecules to degradation. We report here an example in Escherichia coli, where polyadenylation directly controls the level of expression of a gene by modulating the stability of a functional transcript. Inactivation of poly(A)polymerase I causes overexpression of glucosamine–6-phosphate synthase (GlmS) and both the accumulation and stabilization of the glmS transcript. Moreover, we show that the glmS mRNA results from the processing of the glmU-glmS cotranscript by RNase E. Interestingly, the glmU-glmS cotranscript and the mRNA fragment encoding GlmU only slightly accumulated in the absence of poly(A)polymerase, suggesting that the endonucleolytically generated glmS mRNA harbouring a 5' monophosphate and a 3' stable hairpin is highly susceptible to poly(A)-dependent degradation.
Present address: Géraldine Joanny, Laboratory of Diabetes and Experimental Endocrinology Lab.4136 Clinical Science Department, IDIBELL — University of Barcelona Hospital Universitari de Bellvitge, Spain
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