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 8 April 1994:
Vol. 264. no. 5156, pp. 265 - 267
DOI: 10.1126/science.8146659
Prev | Table of Contents | Next

Articles

Science, Vol 264, Issue 5156, 265-267
Copyright © 1994 by American Association for the Advancement of Science

articles

Mutational isolation of a sieve for editing in a transfer RNA synthetase

E Schmidt and P Schimmel

Department of Biology, Massachusetts Institute of Technology, Cambridge 02139.

Editing reactions are essential for the high fidelity of information transfer in processes such as replication, RNA splicing, and protein synthesis. The accuracy of interpretation of the genetic code is enhanced by the editing reactions of aminoacyl transfer RNA (tRNA) synthetases, whereby amino acids are prevented from being attached to the wrong tRNAs. Amino acid discrimination is achieved through sieves that may overlap with or coincide with the amino acid binding site. With the class I Escherichia coli isoleucine tRNA synthetase, which activates isoleucine and occasionally misactivates valine, as an example, a rationally chosen mutant enzyme was constructed that lacks entirely its normal strong ability to distinguish valine from isoleucine by the initial amino acid recognition sieve. The misactivated valine, however, is still eliminated by hydrolytic editing reactions. These data suggest that there is a distinct sieve for editing that is functionally independent of the amino acid binding site.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
An Editing Activity That Prevents Mistranslation and Connection to Disease.
P. Schimmel (2008)
J. Biol. Chem. 283, 28777-28782
   Full Text »    PDF »
Transplantation of a tyrosine editing domain into a tyrosyl-tRNA synthetase variant enhances its specificity for a tyrosine analog.
K. Oki, K. Sakamoto, T. Kobayashi, H. M. Sasaki, and S. Yokoyama (2008)
PNAS 105, 13298-13303
   Abstract »    Full Text »    PDF »
Genetic Code Ambiguity Confers a Selective Advantage on Acinetobacter baylyi.
J. M. Bacher, W. F. Waas, D. Metzgar, V. de Crecy-Lagard, and P. Schimmel (2007)
J. Bacteriol. 189, 6494-6496
   Abstract »    Full Text »    PDF »
Restoring species-specific posttransfer editing activity to a synthetase with a defunct editing domain.
J. SternJohn, S. Hati, P. G. Siliciano, and K. Musier-Forsyth (2007)
PNAS 104, 2127-2132
   Abstract »    Full Text »    PDF »
Pre-transfer Editing by Class II Prolyl-tRNA Synthetase: ROLE OF AMINOACYLATION ACTIVE SITE IN "SELECTIVE RELEASE" OF NONCOGNATE AMINO ACIDS.
S. Hati, B. Ziervogel, J. SternJohn, F.-C. Wong, M. C. Nagan, A. E. Rosen, P. G. Siliciano, J. W. Chihade, and K. Musier-Forsyth (2006)
J. Biol. Chem. 281, 27862-27872
   Abstract »    Full Text »    PDF »
Structural Basis for Non-cognate Amino Acid Discrimination by the Valyl-tRNA Synthetase Editing Domain.
R. Fukunaga and S. Yokoyama (2005)
J. Biol. Chem. 280, 29937-29945
   Abstract »    Full Text »    PDF »
tRNA-dependent Aminoacyl-adenylate Hydrolysis by a Nonediting Class I Aminoacyl-tRNA Synthetase.
I. Gruic-Sovulj, N. Uter, T. Bullock, and J. J. Perona (2005)
J. Biol. Chem. 280, 23978-23986
   Abstract »    Full Text »    PDF »
Archaea recruited D-Tyr-tRNATyr deacylase for editing in Thr-tRNA synthetase.
D. J. RIGDEN (2004)
RNA 10, 1845-1851
   Abstract »    Full Text »    PDF »
Artificially ambiguous genetic code confers growth yield advantage.
V. Pezo, D. Metzgar, T. L. Hendrickson, W. F. Waas, S. Hazebrouck, V. Doring, P. Marliere, P. Schimmel, and V. de Crecy-Lagard (2004)
PNAS 101, 8593-8597
   Abstract »    Full Text »    PDF »
A domain for editing by an archaebacterial tRNA synthetase.
K. Beebe, E. Merriman, L. R. de Pouplana, and P. Schimmel (2004)
PNAS 101, 5958-5963
   Abstract »    Full Text »    PDF »
Functional group recognition at the aminoacylation and editing sites of E. coli valyl-tRNA synthetase.
K. D. TARDIF and J. HOROWITZ (2004)
RNA 10, 493-503
   Abstract »    Full Text »    PDF »
Crystal Structures of the CP1 Domain from Thermus thermophilus Isoleucyl-tRNA Synthetase and Its Complex with L-Valine.
R. Fukunaga, S. Fukai, R. Ishitani, O. Nureki, and S. Yokoyama (2004)
J. Biol. Chem. 279, 8396-8402
   Abstract »    Full Text »    PDF »
Structure-specific tRNA Determinants for Editing a Mischarged Amino Acid.
K. Beebe, E. Merriman, and P. Schimmel (2003)
J. Biol. Chem. 278, 45056-45061
   Abstract »    Full Text »    PDF »
Global Expression Profiling and Physiological Characterization of Corynebacterium glutamicum Grown in the Presence of L-Valine.
C. Lange, D. Rittmann, V. F. Wendisch, M. Bott, and H. Sahm (2003)
Appl. Envir. Microbiol. 69, 2521-2532
   Abstract »    Full Text »    PDF »
Interstice mutations that block site-to-site translocation of a misactivated amino acid bound to a class I tRNA synthetase.
A. C. Bishop, K. Beebe, and P. R. Schimmel (2003)
PNAS 100, 490-494
   Abstract »    Full Text »    PDF »
Crystal structure of a human aminoacyl-tRNA synthetase cytokine.
X.-L. Yang, R. J. Skene, D. E. McRee, and P. Schimmel (2002)
PNAS 99, 15369-15374
   Abstract »    Full Text »    PDF »
Genetic Code Ambiguity. CELL VIABILITY RELATED TO SEVERITY OF EDITING DEFECTS IN MUTANT tRNA SYNTHETASES*.
L. A. Nangle, V. de Crecy Lagard, V. Doring, and P. Schimmel (2002)
J. Biol. Chem. 277, 45729-45733
   Abstract »    Full Text »    PDF »
Transfer RNA determinants for translational editing by Escherichia coli valyl-tRNA synthetase.
K. D. Tardif and J. Horowitz (2002)
Nucleic Acids Res. 30, 2538-2545
   Abstract »    Full Text »    PDF »
Plasticity of Recognition of the 3'-End of Mischarged tRNA by Class I Aminoacyl-tRNA Synthetases.
B. E. Nordin and P. Schimmel (2002)
J. Biol. Chem. 277, 20510-20517
   Abstract »    Full Text »    PDF »
Formation of Two Classes of tRNA Synthetases in Relation to Editing Functions and Genetic Code.
P. SCHIMMEL and L. RIBAS DE POUPLANA (2001)
Cold Spring Harb Symp Quant Biol 66, 161-166
   Abstract »    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 »
Quality Control Mechanisms During Translation.
M. Ibba and a. D. Söll (1999)
Science 286, 1893-1897
   Abstract »    Full Text »
RNA Determinants for Translational Editing. MISCHARGING A MINIHELIX SUBSTRATE BY A tRNA SYNTHETASE.
B. E. Nordin and P. Schimmel (1999)
J. Biol. Chem. 274, 6835-6838
   Abstract »    Full Text »    PDF »
Aminoacyl tRNA synthetases as targets for new anti-infectives.
P. Schimmel, J. Tao, and J. Hill (1998)
FASEB J 12, 1599-1609
   Abstract »    Full Text »
Enzyme Structure with Two Catalytic Sites for Double-Sieve Selection of Substrate.
O. Nureki, D. G. Vassylyev, M. Tateno, A. Shimada, T. Nakama, S. Fukai, M. Konno, T. L. Hendrickson, P. Schimmel, and S. Yokoyama (1998)
Science 280, 578-582
   Abstract »    Full Text »
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 »
Blocking site-to-site translocation of a misactivated amino acid by mutation of a class I tRNA synthetase.
A. C. Bishop, T. K. Nomanbhoy, and P. Schimmel (2002)
PNAS 99, 585-590
   Abstract »    Full Text »    PDF »
Misactivated amino acids translocate at similar rates across surface of a tRNA synthetase.
T. K. Nomanbhoy and P. R. Schimmel (2000)
PNAS 97, 5119-5122
   Abstract »    Full Text »    PDF »


To Advertise     Find Products

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