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Science 21 January 2000:
Vol. 287. no. 5452, pp. 479 - 482
DOI: 10.1126/science.287.5452.479
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Reports

One Polypeptide with Two Aminoacyl-tRNA Synthetase Activities

Constantinos Stathopoulos, 1 Tong Li, 1 Randy Longman, 1 Ute C. Vothknecht, 1 Hubert D. Becker, 1 Michael Ibba, 4 Dieter Söll 123*

The genome sequences of certain archaea do not contain recognizable cysteinyl-transfer RNA (tRNA) synthetases, which are essential for messenger RNA-encoded protein synthesis. However, a single cysteinyl-tRNA synthetase activity was detected and purified from one such organism, Methanococcus jannaschii. The amino-terminal sequence of this protein corresponded to the predicted sequence of prolyl-tRNA synthetase. Biochemical and genetic analyses indicated that this archaeal form of prolyl-tRNA synthetase can synthesize both cysteinyl-tRNACys and prolyl-tRNAPro. The ability of one enzyme to provide two aminoacyl-tRNAs for protein synthesis raises questions about concepts of substrate specificity in protein synthesis and may provide insights into the evolutionary origins of this process.

1 Departments of Molecular Biophysics and Biochemistry;
2 Chemistry; and
3 Molecular, Cellular and Developmental Biology, Yale University, New Haven, CT 06520-8114, USA.
4 Center for Biomolecular Recognition, Department of Medical Biochemistry and Genetics, Laboratory B, Panum Institute, Blegdamsvej 3c, DK-2200, Copenhagen N, Denmark.
*   To whom correspondence should be addressed at the Department of Molecular Biophysics and Biochemistry, Yale University, Post Office Box 208114, 266 Whitney Avenue, New Haven, CT 06520-8114, USA. E-mail: soll{at}trna.chem.yale.edu

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