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.

Site Tools

  • AAAS
  • Subscribe
  • Feedback

Site Search

Search Advanced

Science 23 December 1988:
Vol. 242. no. 4886, pp. 1681 - 1684
DOI: 10.1126/science.2462282
Prev | Table of Contents | Next

Articles

Science, Vol 242, Issue 4886, 1681-1684
Copyright © 1988 by American Association for the Advancement of Science

articles

Association of transfer RNA acceptor identity with a helical irregularity

WH McClain, YM Chen, K Foss, and J Schneider

Department of Bacteriology, University of Wisconsin, Madison 53706.

The aminoacylation specificity ("acceptor identity") of transfer RNAs (tRNAs) has previously been associated with the position of particular nucleotides, as opposed to distinctive elements of three-dimensional structure. The contribution of a G.U wobble pair in the acceptor helix of tRNA(Ala) to acceptor identity was examined with synthetic amber suppressor tRNAs in Escherichia coli. The acceptor identity was not affected by replacing the G.U wobble pair in tRNA(Ala) with a G.A, C.A, or U.U wobble pair. Furthermore, a tRNA(Ala) acceptor identity was conferred on tRNA(Lys) when the same site in the acceptor helix was replaced with any of several wobble pairs. Additional data with tRNA(Ala) show that a substantial acceptor identity was retained when the G.U wobble pair was translocated to another site in the acceptor helix. These results suggest that the G.U wobble pair induces an irregularity in the acceptor helix of tRNA(Ala) to match a complementary structure in the aminoacylating enzyme.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Misacylation of Yeast Amber Suppressor tRNATyr by E. coli Lysyl-tRNA Synthetase and Its Effective Repression by Genetic Engineering of the tRNA Sequence..
J.-i. Fukunaga, T. Yokogawa, S. Ohno, and K. Nishikawa (2006)
J. Biochem. 139, 689-696
   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 »
Uniform Binding of Aminoacyl-tRNAs to Elongation Factor Tu by Thermodynamic Compensation.
F. J. LaRiviere, A. D. Wolfson, and O. C. Uhlenbeck (2001)
Science 294, 165-168
   Abstract »    Full Text »    PDF »
Hydrolytic editing by a class II aminoacyl-tRNA synthetase.
P. J. Beuning and K. Musier-Forsyth (2000)
PNAS 97, 8916-8920
   Abstract »    Full Text »    PDF »
Correlation of deformability at a tRNA recognition site and aminoacylation specificity.
K.-Y. Chang, G. Varani, S. Bhattacharya, H. Choi, and W. H. McClain (1999)
PNAS 96, 11764-11769
   Abstract »    Full Text »    PDF »
Specific atomic groups and RNA helix geometry in acceptor stem recognition by a tRNA synthetase.
P. J. Beuning, F. Yang, P. Schimmel, and K. Musier-Forsyth (1997)
PNAS 94, 10150-10154
   Abstract »    Full Text »    PDF »
Specificity for aminoacylation of an RNA helix: an unpaired, exocyclic amino group in the minor groove.
K Musier-Forsyth, N Usman, S Scaringe, J Doudna, R Green, and P Schimmel (1991)
Science 253, 784-786
   Abstract »    PDF »
Structural basis for misaminoacylation by mutant E. coli glutaminyl-tRNA synthetase enzymes.
J. Perona, R. Swanson, M. Rould, T. Steitz, and D Soll (1989)
Science 246, 1152-1154
   Abstract »    PDF »
Species-specific Differences in Amino Acid Editing by Class II Prolyl-tRNA Synthetase.
P. J. Beuning and K. Musier-Forsyth (2001)
J. Biol. Chem. 276, 30779-30785
   Abstract »    Full Text »    PDF »


To Advertise     Find Products

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