Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.


Science 13 March 1998:
Vol. 279. no. 5357, pp. 1665 - 1670
DOI: 10.1126/science.279.5357.1665

Research Articles

Evolution of a Transfer RNA Gene Through a Point Mutation in the Anticodon

Margaret E. Saks, *dagger Jeffrey R. Sampson, ddagger John Abelson

The transfer RNA (tRNA) multigene family comprises 20 amino acid-accepting groups, many of which contain isoacceptors. The addition of isoacceptors to the tRNA repertoire was critical to establishing the genetic code, yet the origin of isoacceptors remains largely unexplored. A model of tRNA evolution, termed "tRNA gene recruitment," was formulated. It proposes that a tRNA gene can be recruited from one isoaccepting group to another by a point mutation that concurrently changes tRNA amino acid identity and messenger RNA coupling capacity. A test of the model showed that an Escherichia coli strain, in which the essential tRNAUGUThr gene was inactivated, was rendered viable when a tRNAArg with a point mutation that changed its anticodon from UCU to UGU (threonine) was expressed. Insertion of threonine at threonine codons by the "recruited" tRNAArg was corroborated by in vitro aminoacylation assays showing that its specificity had been changed from arginine to threonine. Therefore, the recruitment model may account for the evolution of some tRNA genes.

Division of Biology 147-75, California Institute of Technology, Pasadena, CA 91125, USA.
*   To whom correspondence should be addressed. E-mail: peggy{at}seqaxp.bio.caltech.edu

dagger    Present address: Department of Biology, University of Oregon, Eugene, OR 97403, USA.

ddagger    Present address: Hewlett-Packard Laboratories, 3500 Deer Creek Road, Mail Stop 25U-5, Palo Alto, CA 94304, USA.


Read the Full Text


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Low modularity of aminoacyl-tRNA substrates in polymerization by the ribosome.
A. C. Forster (2009)
Nucleic Acids Res. 37, 3747-3755
   Abstract »    Full Text »    PDF »
Coevolution of Codon Usage and tRNA Genes Leads to Alternative Stable States of Biased Codon Usage.
P. G. Higgs and W. Ran (2008)
Mol. Biol. Evol. 25, 2279-2291
   Abstract »    Full Text »    PDF »
In silico detection of tRNA sequence features characteristic to aminoacyl-tRNA synthetase class membership.
E. Jako, P. Ittzes, A. Szenes, A. Kun, E. Szathmary, and G. Pal (2007)
Nucleic Acids Res.
   Abstract »    Full Text »    PDF »
Anticodon-dependent conservation of bacterial tRNA gene sequences.
M. E. Saks and J. S. Conery (2007)
RNA 13, 651-660
   Abstract »    Full Text »    PDF »
TFAM detects co-evolution of tRNA identity rules with lateral transfer of histidyl-tRNA synthetase.
D. H. Ardell and S. G. E. Andersson (2006)
Nucleic Acids Res. 34, 893-904
   Abstract »    Full Text »    PDF »
Loss of Editing Activity during the Evolution of Mitochondrial Phenylalanyl-tRNA Synthetase.
H. Roy, J. Ling, J. Alfonzo, and M. Ibba (2005)
J. Biol. Chem. 280, 38186-38192
   Abstract »    Full Text »    PDF »
A yeast arginine specific tRNA is a remnant aspartate acceptor.
A. Fender, R. Geslain, G. Eriani, R. Giege, M. Sissler, and C. Florentz (2004)
Nucleic Acids Res. 32, 5076-5086
   Abstract »    Full Text »    PDF »
Changing identities: tRNA duplication and remolding within animal mitochondrial genomes.
T. A. Rawlings, T. M. Collins, and R. Bieler (2003)
PNAS 100, 15700-15705
   Abstract »    Full Text »    PDF »
Modulation of tRNAAla identity by inorganic pyrophosphatase.
A. D. Wolfson and O. C. Uhlenbeck (2002)
PNAS 99, 5965-5970
   Abstract »    Full Text »    PDF »
Making sense out of nonsense.
M. E. Saks (2001)
PNAS 98, 2125-2127
   Full Text »    PDF »
Testing a biosynthetic theory of the genetic code: Fact or artifact?.
T. A. Ronneberg, L. F. Landweber, and S. J. Freeland (2000)
PNAS
   Abstract »    Full Text »
Aminoacyl-tRNA Synthetases, the Genetic Code, and the Evolutionary Process.
C. R. Woese, G. J. Olsen, M. Ibba, and D. Soll (2000)
Microbiol. Mol. Biol. Rev. 64, 202-236
   Abstract »    Full Text »    PDF »
A Mutation in GRS1, a Glycyl-tRNA Synthetase, Affects 3'-End Formation in Saccharomyces cerevisiae.
C. Magrath and L. E. Hyman (1999)
Genetics 152, 129-141
   Abstract »    Full Text »
Substrate recognition by class I lysyl-tRNA synthetases: A molecular basis for gene displacement.
M. Ibba, H. C. Losey, Y. Kawarabayasi, H. Kikuchi, S. Bunjun, and D. Soll (1999)
PNAS 96, 418-423
   Abstract »    Full Text »    PDF »
Linkage Map of Escherichia coli K-12, Edition 10: The Traditional Map.
M. K. B. Berlyn (1998)
Microbiol. Mol. Biol. Rev. 62, 814-984
   Abstract »    Full Text »    PDF »
Testing a biosynthetic theory of the genetic code: Fact or artifact?.
T. A. Ronneberg, L. F. Landweber, and S. J. Freeland (2000)
PNAS 97, 13690-13695
   Abstract »    Full Text »    PDF »



To Advertise     Find Products


Science. ISSN 0036-8075 (print), 1095-9203 (online)