JBC PeproTech; Our Business is Cytokines!

HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


Originally published In Press as doi:10.1074/jbc.M111825200 on January 4, 2002

J. Biol. Chem., Vol. 277, Issue 11, 8835-8840, March 15, 2002
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
277/11/8835    most recent
M111825200v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Agarwalla, S.
Right arrow Articles by Stroud, R. M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Agarwalla, S.
Right arrow Articles by Stroud, R. M.
Social Bookmarking
 Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

Characterization of the 23 S Ribosomal RNA m5U1939 Methyltransferase from Escherichia coli*

Sanjay Agarwalla, James T. KealeyDagger , Daniel V. SantiDagger , and Robert M. Stroud§

From the Departments of Biochemistry and Biophysics and Pharmaceutical Chemistry, University of California at San Francisco, San Francisco, California 94143-0448

An Escherichia coli open reading frame, ygcA, was identified as a putative 23 S ribosomal RNA 5-methyluridine methyltransferase (Gustafsson, C., Reid, R., Greene, P. J., and Santi, D. V. (1996) Nucleic Acids Res. 24, 3756-3762). We have cloned, expressed, and purified the 50-kDa protein encoded by ygcA. The purified enzyme catalyzed the AdoMet-dependent methylation of 23 S rRNA but did not act upon 16 S rRNA or tRNA. A high performance liquid chromatography-based nucleoside analysis identified the reaction product as 5-methyluridine. The enzyme specifically methylated U1939 as determined by a nuclease protection assay and by methylation assays using site-specific mutants of 23 S rRNA. A 40-nucleotide 23 S rRNA fragment (nucleotide 1930-1969) also served as an efficient substrate for the enzyme. The apparent Km values for the 40-mer RNA oligonucleotide and AdoMet were 3 and 26 µM, respectively, and the apparent kcat was 0.06 s-1. The enzyme contains two equivalents of iron/monomer and has a sequence motif similar to a motif found in iron-sulfur proteins. We propose to name this gene rumA and accordingly name the protein product as RumA for RNA uridine methyltransferase.


* This work was supported by the United States Public Health Service, National Institutes of Health Grant GM51232 (to R. M. S.).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.

Dagger Present address: Kosan Biosciences, Inc., 3832 Bay Center Place, Hayward, CA 94545.

§ To whom correspondence should be addressed: Dept. of Biochemistry and Biophysics, University of California at San Francisco, San Francisco, California 94143-0448. Tel.: 415-476-4224; Fax: 415-476-1902; E-mail: stroud@msg.ucsf.edu.


Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
J. Bacteriol.Home page
M. Savic, T. Ilic-Tomic, R. Macmaster, B. Vasiljevic, and G. L. Conn
Critical Residues for Cofactor Binding and Catalytic Activity in the Aminoglycoside Resistance Methyltransferase Sgm
J. Bacteriol., September 1, 2008; 190(17): 5855 - 5861.
[Abstract] [Full Text] [PDF]


Home page
Nucleic Acids ResHome page
H. Walbott, N. Leulliot, H. Grosjean, and B. Golinelli-Pimpaneau
The crystal structure of Pyrococcus abyssi tRNA (uracil-54, C5)-methyltransferase provides insights into its tRNA specificity
Nucleic Acids Res., September 1, 2008; 36(15): 4929 - 4940.
[Abstract] [Full Text] [PDF]


Home page
Proc. Natl. Acad. Sci. USAHome page
A. Alian, T. T. Lee, S. L. Griner, R. M. Stroud, and J. Finer-Moore
Structure of a TrmA-RNA complex: A consensus RNA fold contributes to substrate selectivity and catalysis in m5U methyltransferases
PNAS, May 13, 2008; 105(19): 6876 - 6881.
[Abstract] [Full Text] [PDF]


Home page
J. Bacteriol.Home page
J. Wang, N. Gardiol, T. Burr, G. P. C. Salmond, and M. Welch
RelA-Dependent (p)ppGpp Production Controls Exoenzyme Synthesis in Erwinia carotovora subsp. atroseptica
J. Bacteriol., November 1, 2007; 189(21): 7643 - 7652.
[Abstract] [Full Text] [PDF]


Home page
RNAHome page
G. N. Basturea and M. P. Deutscher
Substrate specificity and properties of the Escherichia coli 16S rRNA methyltransferase, RsmE
RNA, November 1, 2007; 13(11): 1969 - 1976.
[Abstract] [Full Text] [PDF]


Home page
Nucleic Acids ResHome page
J. Urbonavicius, G. Jager, and G. R. Bjork
Amino acid residues of the Escherichia coli tRNA(m5U54)methyltransferase (TrmA) critical for stability, covalent binding of tRNA and enzymatic activity
Nucleic Acids Res., May 11, 2007; 35(10): 3297 - 3305.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
S. Hur, R. M. Stroud, and J. Finer-Moore
Substrate Recognition by RNA 5-Methyluridine Methyltransferases and Pseudouridine Synthases: A Structural Perspective
J. Biol. Chem., December 22, 2006; 281(51): 38969 - 38973.
[Full Text] [PDF]


Home page
Nucleic Acids ResHome page
J. Urbonavicius, S. Skouloubris, H. Myllykallio, and H. Grosjean
Identification of a novel gene encoding a flavin-dependent tRNA:m5U methyltransferase in bacteria--evolutionary implications
Nucleic Acids Res., July 18, 2005; 33(13): 3955 - 3964.
[Abstract] [Full Text] [PDF]


Home page
RNAHome page
B. HUANG, M. J.O. JOHANSSON, and A. S. BYSTROM
An early step in wobble uridine tRNA modification requires the Elongator complex
RNA, April 1, 2005; 11(4): 424 - 436.
[Abstract] [Full Text] [PDF]


Home page
J. Bacteriol.Home page
J. Hager, B. L. Staker, and U. Jakob
Substrate Binding Analysis of the 23S rRNA Methyltransferase RrmJ
J. Bacteriol., October 1, 2004; 186(19): 6634 - 6642.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
S. Agarwalla, R. M. Stroud, and B. J. Gaffney
Redox Reactions of the Iron-Sulfur Cluster in a Ribosomal RNA Methyltransferase, RumA: OPTICAL AND EPR STUDIES
J. Biol. Chem., August 13, 2004; 279(33): 34123 - 34129.
[Abstract] [Full Text] [PDF]


Home page
Nucleic Acids ResHome page
C. T. Madsen, J. Mengel-Jorgensen, F. Kirpekar, and S. Douthwaite
Identifying the methyltransferases for m5U747 and m5U1939 in 23S rRNA using MALDI mass spectrometry
Nucleic Acids Res., August 15, 2003; 31(16): 4738 - 4746.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 2002 by the American Society for Biochemistry and Molecular Biology.