Human tRNA synthetase catalytic nulls with diverse functions-Reference-Cited by-同舟云学术

Human tRNA synthetase catalytic nulls with diverse functions

Published:2014-07-18 Issue:6194 Volume:345 Page:328-332
ISSN:0036-8075
Container-title:Science
language:en
Short-container-title:Science

Author:

Lo Wing-Sze¹²,Gardiner Elisabeth³⁴,Xu Zhiwen¹²,Lau Ching-Fun¹²,Wang Feng¹²,Zhou Jie J.¹²,Mendlein John D.⁴,Nangle Leslie A.⁴,Chiang Kyle P.⁴,Yang Xiang-Lei¹³,Au Kin-Fai⁵,Wong Wing Hung⁶,Guo Min⁷,Zhang Mingjie¹⁸,Schimmel Paul¹³⁷

Affiliation:

1. IAS HKUST–Scripps R&D Laboratory, Institute for Advanced Study, Hong Kong University of Science and Technology, Clear Water Bay, Kowloon, Hong Kong, China.

2. Pangu Biopharma, Edinburgh Tower, The Landmark, 15 Queen’s Road Central, Hong Kong, China.

3. The Scripps Laboratories for tRNA Synthetase Research, The Scripps Research Institute, 10650 North Torrey Pines Road, La Jolla, CA 92037, USA.

4. aTyr Pharma, 3545 John Hopkins Court, Suite 250, San Diego, CA 92121, USA.

5. Department of Internal Medicine, University of Iowa, Iowa City, IA 52242, USA.

6. Department of Statistics, Stanford University, Stanford, CA 94305, USA.

7. The Scripps Laboratories for tRNA Synthetase Research, Scripps Florida, 130 Scripps Way, Jupiter, FL 33458, USA.

8. Division of Life Science, State Key Laboratory of Molecular Neuroscience, Hong Kong University of Science and Technology, Clear Water Bay, Kowloon, Hong Kong, China.

Abstract

Evolving from an enzyme and into a regulator Proteins, the work-horses of the cell, are made on a messenger RNA (mRNA) template. An enzyme called aminoacyl tRNA synthetases (AARSs) attaches the correct amino acid to a transfer RNA so that mRNA is accurately translated. Over evolution, additional sequences have been added to AARSs. Lo et al. found a large number of AARS variants in which the domain responsible for enzyme function was deleted. Ninety-four such variants had diverse signaling activities. Thus, AARSs are used both as enzymes and alternately as regulators of signaling pathways. Science , this issue p. 328

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

Reference34 articles.

1. CP1-dependent partitioning of pretransfer and posttransfer editing in leucyl-tRNA synthetase

2. The return of pretransfer editing in protein synthesis

3. Genetic code expansion

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5. Aminoacyl-tRNAs: setting the limits of the genetic code

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