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Science 2 April 1999:
Vol. 284. no. 5411, pp. 63 - 64
DOI: 10.1126/science.284.5411.63

Perspectives

Also see the archival list of Science's Compass: Enhanced Perspectives

EVOLUTION:
Enhanced: A Deadly Double Life

Alan M. Weiner and Nancy Maizels

The human tyrosyl-tRNA synthetase, an enzyme that connects the amino acid tyrosine with its correct tRNA in preparation for protein synthesis, seems to have a totally different function according to Wakasugi and Schimmel, reporting in this issue. In a Perspective on this work, Weiner and Maizels explain that as cells undergo programmed cell death (apoptosis), tyrosyl-tRNA synthetase is secreted and cleaved into two fragments, each with cytokine activity. Weiner and Maizels speculate that the cytokines might encourage phagocytic cells such as macrophages to arrive at the scene of apoptosis and clear up the cell corpses. The authors also discuss the evolution of this dual existence as the EMAPII-like domain is conserved in the tRNA synthetases of bacteria, yeast, and worms.


The authors are in the Departments of Molecular Biophysics and Biochemistry, and Genetics, Yale University School of Medicine, New Haven, CT 06520-8024, USA. E-mail: weiner{at}biomed.med.yale.edu; nancy.maizels{at}yale.edu

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THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Quantitative Proteomic Analysis of Myc-induced Apoptosis: A DIRECT ROLE FOR Myc INDUCTION OF THE MITOCHONDRIAL CHLORIDE ION CHANNEL, mtCLIC/CLIC4.
Y. Shiio, K. S. Suh, H. Lee, S. H. Yuspa, R. N. Eisenman, and R. Aebersold (2006)
J. Biol. Chem. 281, 2750-2756
   Abstract »    Full Text »    PDF »
Aminoacyl-tRNA synthetases database Y2K.
M. Szymanski and J. Barciszewski (2000)
Nucleic Acids Res. 28, 326-328
   Abstract »    Full Text »    PDF »
Evolution of Aminoacyl-tRNA Synthetases---Analysis of Unique Domain Architectures and Phylogenetic Trees Reveals a Complex History of Horizontal Gene Transfer Events.
Y. I. Wolf, L. Aravind, N. V. Grishin, and E. V. Koonin (1999)
Genome Res. 9, 689-710
   Abstract »    Full Text »
The Cytokine Portion of p43 Occupies a Central Position within the Eukaryotic Multisynthetase Complex.
M. T. Norcum and J. A. Warrington (2000)
J. Biol. Chem. 275, 17921-17924
   Abstract »    Full Text »    PDF »
Arc1p Organizes the Yeast Aminoacyl-tRNA Synthetase Complex and Stabilizes Its Interaction with the Cognate tRNAs.
K. Deinert, F. Fasiolo, E. C. Hurt, and G. Simos (2001)
J. Biol. Chem. 276, 6000-6008
   Abstract »    Full Text »    PDF »



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