JBC

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


     

Originally published In Press as doi:10.1074/jbc.M109494200 on October 3, 2001

J. Biol. Chem., Vol. 276, Issue 49, 45862-45867, December 7, 2001
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
276/49/45862    most recent
M109494200v1
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 Raczniak, G.
Right arrow Articles by Söll, D.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Raczniak, G.
Right arrow Articles by Söll, D.
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?

A Single Amidotransferase Forms Asparaginyl-tRNA and Glutaminyl-tRNA in Chlamydia trachomatis*

Gregory RaczniakDagger §, Hubert D. BeckerDagger , Bokkee MinDagger , and Dieter SöllDagger ||**

From the Dagger  Department of Molecular Biophysics and Biochemistry and || Chemistry, Yale University, New Haven, Connecticut 06520-8114

Aminoacyl-tRNA is generally formed by aminoacyl-tRNA synthetases, a family of 20 enzymes essential for accurate protein synthesis. However, most bacteria generate one of the two amide aminoacyl-tRNAs, Asn-tRNA or Gln-tRNA, by transamidation of mischarged Asp-tRNAAsn or Glu-tRNAGln catalyzed by a heterotrimeric amidotransferase (encoded by the gatA, gatB, and gatC genes). The Chlamydia trachomatis genome sequence reveals genes for 18 synthetases, whereas those for asparaginyl-tRNA synthetase and glutaminyl-tRNA synthetase are absent. Yet the genome harbors three gat genes in an operon-like arrangement (gatCAB). We reasoned that Chlamydia uses the gatCAB-encoded amidotransferase to generate both Asn-tRNA and Gln-tRNA. C. trachomatis aspartyl-tRNA synthetase and glutamyl-tRNA synthetase were shown to be non-discriminating synthetases that form the misacylated tRNAAsn and tRNAGln species. A preparation of pure heterotrimeric recombinant C. trachomatis amidotransferase converted Asp-tRNAAsn and Glu-tRNAGln into Asn-tRNA and Gln-tRNA, respectively. The enzyme used glutamine, asparagine, or ammonia as amide donors in the presence of either ATP or GTP. These results suggest that C. trachomatis employs the dual specificity gatCAB-encoded amidotransferase and 18 aminoacyl-tRNA synthetases to create the complete set of 20 aminoacyl-tRNAs.

* Supported by a grant from the NIGMS, National Institutes of Health.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.

§ A predoctoral fellow of the Heyl Foundation. Present address: Eastern Virginia Medical School, 721 Fairfax Avenue, Norfolk, VA 23507-2000.

A European Molecular Biology postdoctoral fellow.

** To whom correspondence should be addressed: Dept. of Molecular Biophysics and Biochemistry, Yale University, P. O. Box 208114, 266 Whitney Ave., New Haven, CT 06520-8114. Tel.: 203-432-6200; Fax: 203-432-6202; E-mail: soll@trna.chem.yale.edu.

Copyright © 2001 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
 Nucleic Acids ResHome page
K. Sheppard, J. Yuan, M. J. Hohn, B. Jester, K. M. Devine, and D. Soll
From one amino acid to another: tRNA-dependent amino acid biosynthesis
Nucleic Acids Res., April 1, 2008; 36(6): 1813 - 1825.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
K. Sheppard, P.-M. Akochy, J. C. Salazar, and D. Soll
The Helicobacter pylori Amidotransferase GatCAB Is Equally Efficient in Glutamine-dependent Transamidation of Asp-tRNAAsn and Glu-tRNAGln
J. Biol. Chem., April 20, 2007; 282(16): 11866 - 11873.
[Abstract] [Full Text] [PDF]

Home page
 J. Bacteriol.Home page
P. Xu, J. M. Alves, T. Kitten, A. Brown, Z. Chen, L. S. Ozaki, P. Manque, X. Ge, M. G. Serrano, D. Puiu, et al.
Genome of the Opportunistic Pathogen Streptococcus sanguinis
J. Bacteriol., April 15, 2007; 189(8): 3166 - 3175.
[Abstract] [Full Text] [PDF]

Home page
 Nucleic Acids ResHome page
M. Deniziak, C. Sauter, H. D. Becker, C. A. Paulus, R. Giege, and D. Kern
Deinococcus glutaminyl-tRNA synthetase is a chimer between proteins from an ancient and the modern pathways of aminoacyl-tRNA formation
Nucleic Acids Res., March 12, 2007; 35(5): 1421 - 1431.
[Abstract] [Full Text] [PDF]

Home page
 Nucleic Acids ResHome page
M. Bailly, S. Giannouli, M. Blaise, C. Stathopoulos, D. Kern, and H. D. Becker
A single tRNA base pair mediates bacterial tRNA-dependent biosynthesis of asparagine
Nucleic Acids Res., December 4, 2006; 34(21): 6083 - 6094.
[Abstract] [Full Text] [PDF]

Home page
 ScienceHome page
H. Oshikane, K. Sheppard, S. Fukai, Y. Nakamura, R. Ishitani, T. Numata, R. L. Sherrer, L. Feng, E. Schmitt, M. Panvert, et al.
Structural basis of RNA-dependent recruitment of glutamine to the genetic code.
Science, June 30, 2006; 312(5782): 1950 - 1954.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
J. Sabina and D. Soll
The RNA-binding PUA Domain of Archaeal tRNA-Guanine Transglycosylase Is Not Required for Archaeosine Formation
J. Biol. Chem., March 17, 2006; 281(11): 6993 - 7001.
[Abstract] [Full Text] [PDF]

Home page
 J. Bacteriol.Home page
D. Bernard, P.-M. Akochy, D. Beaulieu, J. Lapointe, and P. H. Roy
Two Residues in the Anticodon Recognition Domain of the Aspartyl-tRNA Synthetase from Pseudomonas aeruginosa Are Individually Implicated in the Recognition of tRNAAsn
J. Bacteriol., January 1, 2006; 188(1): 269 - 274.
[Abstract] [Full Text] [PDF]

Home page
 Proc. Natl. Acad. Sci. USAHome page
J. C. Salazar, A. Ambrogelly, P. F. Crain, J. A. McCloskey, and D. Soll
From The Cover: A truncated aminoacyl-tRNA synthetase modifies RNA
PNAS, May 18, 2004; 101(20): 7536 - 7541.
[Abstract] [Full Text] [PDF]

Home page
 Genes Dev.Home page
M. Ibba and D. Soll
Aminoacyl-tRNAs: setting the limits of the genetic code
Genes & Dev., April 1, 2004; 18(7): 731 - 738.
[Full Text] [PDF]

Home page
 J. Bacteriol.Home page
P.-M. Akochy, D. Bernard, P. H. Roy, and J. Lapointe
Direct Glutaminyl-tRNA Biosynthesis and Indirect Asparaginyl-tRNA Biosynthesis in Pseudomonas aeruginosa PAO1
J. Bacteriol., February 1, 2004; 186(3): 767 - 776.
[Abstract] [Full Text] [PDF]

Home page
 Proc. Natl. Acad. Sci. USAHome page
J. C. Salazar, I. Ahel, O. Orellana, D. Tumbula-Hansen, R. Krieger, L. Daniels, and D. Soll
Coevolution of an aminoacyl-tRNA synthetase with its tRNA substrates
PNAS, November 25, 2003; 100(24): 13863 - 13868.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
A. Brevet, J. Chen, S. Commans, C. Lazennec, S. Blanquet, and P. Plateau
Anticodon Recognition in Evolution: SWITCHING tRNA SPECIFICITY OF AN AMINOACYL-tRNA SYNTHETASE BY SITE-DIRECTED PEPTIDE TRANSPLANTATION
J. Biol. Chem., August 15, 2003; 278(33): 30927 - 30935.
[Abstract] [Full Text] [PDF]

Home page
 Genome ResHome page
D. Raoult, H. Ogata, S. Audic, C. Robert, K. Suhre, M. Drancourt, and J.-M. Claverie
Tropheryma whipplei Twist: A Human Pathogenic Actinobacteria With a Reduced Genome
Genome Res., August 1, 2003; 13(8): 1800 - 1809.
[Abstract] [Full Text] [PDF]

Home page
 J. Bacteriol.Home page
B. Min, M. Kitabatake, C. Polycarpo, J. Pelaschier, G. Raczniak, B. Ruan, H. Kobayashi, S. Namgoong, and D. Soll
Protein Synthesis in Escherichia coli with Mischarged tRNA
J. Bacteriol., June 15, 2003; 185(12): 3524 - 3526.
[Abstract] [Full Text] [PDF]

Home page
 Proc. Natl. Acad. Sci. USAHome page
L. Feng, D. Tumbula-Hansen, H. Toogood, and D. Soll
Expanding tRNA recognition of a tRNA synthetase by a single amino acid change
PNAS, May 13, 2003; 100(10): 5676 - 5681.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
M. Ryckelynck, R. Giege, and M. Frugier
Yeast tRNAAsp Charging Accuracy Is Threatened by the N-terminal Extension of Aspartyl-tRNA Synthetase
J. Biol. Chem., March 7, 2003; 278(11): 9683 - 9690.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
D. Tumbula-Hansen, L. Feng, H. Toogood, K. O. Stetter, and D. Soll
Evolutionary Divergence of the Archaeal Aspartyl-tRNA Synthetases into Discriminating and Nondiscriminating Forms
J. Biol. Chem., September 27, 2002; 277(40): 37184 - 37190.
[Abstract] [Full Text] [PDF]

Home page
 Proc. Natl. Acad. Sci. USAHome page
B. Min, J. T. Pelaschier, D. E. Graham, D. Tumbula-Hansen, and D. Soll
Transfer RNA-dependent amino acid biosynthesis: An essential route to asparagine formation
PNAS, March 5, 2002; 99(5): 2678 - 2683.
[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 © 2001 by the American Society for Biochemistry and Molecular Biology.