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J. Biol. Chem., Vol. 277, Issue 38, 34743-34748, September 20, 2002
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From the Departments of Aminoacyl-tRNA synthetases are well known for
their remarkable precision in substrate selection during aminoacyl-tRNA
formation. Some synthetases enhance the accuracy of this process by
editing mechanisms that lead to hydrolysis of incorrectly activated
and/or charged amino acids. Prolyl-tRNA synthetases (ProRSs) can be
divided into two structurally divergent groups, archaeal-type and
bacterial-type enzymes. A striking difference between these groups is
the presence of an insertion domain (~180 amino acids) in the
bacterial-type ProRS. Because the archaeal-type ProRS enzymes have been
shown to recognize cysteine, we tested selected ProRSs from all three domains of life to determine whether cysteine activation is a general
property of ProRS. Here we show that cysteine is activated by
recombinant ProRS enzymes from the archaea Methanocaldococcus jannaschii and Methanothermobacter
thermautotrophicus, from the eukaryote Saccharomyces
cerevisiae, and from the bacteria Aquifex aeolicus,
Borrelia burgdorferi, Clostridium sticklandii, Cytophaga hutchinsonii, Deinococcus radiodurans, Escherichia coli,
Magnetospirillum magnetotacticum, Novosphingobium aromaticivorans,
Rhodopseudomonas palustris, and Thermus thermophilus.
This non-cognate amino acid was efficiently acylated in
vitro onto tRNAPro, and the misacylated
Cys-tRNAPro was not edited by ProRS. Therefore, ProRS
exhibits a natural level of mischarging that is to date unequalled
among the aminoacyl-tRNA synthetases.
Cysteine Activation Is an Inherent in Vitro Property
of Prolyl-tRNA Synthetases*
,,,,,¶
Molecular Biophysics and
Biochemistry and ¶ Chemistry, Yale University, New Haven,
Connecticut 06520-8114 and the § Institut für
Mikrobiologie und Genetik der Universität Göttingen,
D-37077 Göttingen, Germany
*
This work was supported by grants from the NIGMS, National
Institutes of Health, the Department of Energy, and the National Aeronautics and Space Administration.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.
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.
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