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Originally published In Press as doi:10.1074/jbc.M001854200 on March 19, 2000

J. Biol. Chem., Vol. 275, Issue 22, 16414-16419, June 2, 2000
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The FtsJ/RrmJ Heat Shock Protein of Escherichia coli Is a 23 S Ribosomal RNA Methyltransferase*

Teresa CaldasDagger §, Emmanuelle Binet, Philippe Bouloc, Annie Costa||, Jean Desgres||, and Gilbert RicharmeDagger **

From Dagger  Biochimie Génétique, Institut Jacques Monod, Université Paris 7, 2, place Jussieu, 75005 Paris,  Laboratoire des Réseaux de Régulations, Institut de Génétique et Microbiologie, Université Paris-Sud, CNRS, UMR8621, 91405 Orsay Cedex, and || Laboratoire de Biochimie Médicale, Faculté de Médecine et Centre Hospitalier de Bourgogne, 10 boulevard de Lattre de Tassigny, 21034 Dijon, France

Ribosomal RNAs undergo several nucleotide modifications including methylation. We identify FtsJ, the first encoded protein of the ftsJ-hflB heat shock operon, as an Escherichia coli methyltransferase of the 23 S rRNA. The methylation reaction requires S-adenosylmethionine as donor of methyl groups, purified FtsJ or a S150 supernatant from an FtsJ-producing strain, and ribosomes from an FtsJ-deficient strain. In vitro, FtsJ does not efficiently methylate ribosomes purified from a strain producing FtsJ, suggesting that these ribosomes are already methylated in vivo by FtsJ. FtsJ is active on ribosomes and on the 50 S ribosomal subunit, but is inactive on free rRNA, suggesting that its natural substrate is ribosomes or a pre-ribosomal ribonucleoprotein particle. We identified the methylated nucleotide as 2'-O-methyluridine 2552, by reverse phase high performance liquid chromatography analysis, boronate affinity chromatography, and hybridization-protection experiments. In view of its newly established function, FtsJ is renamed RrmJ and its encoding gene, rrmJ.


* This work was supported in part by the Programme de Recherche Fondamentale en Microbiologie, Maladies Infectieuses et Parasitaires, funded by the Ministère de L'Education Nationale, de la Recherche et de la Technologie, and by Association pour la Recherche sur le Cancer Grant 9956.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

§ Supported by Fundaçao para a Ciéncia e Tecnologia of Portugal Grant PRAXIS/BD/13898/97.

** To whom correspondence should be addressed. Tel.: 33-1-44-27-50-98; Fax: 33-1-44-27-35-80; E-mail: richarme@ccr.jussieu.fr.


Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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