A paralog of lysyl-tRNA synthetase aminoacylates a conserved lysine residue in translation elongation factor P-Reference-Cited by-同舟云学术

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A paralog of lysyl-tRNA synthetase aminoacylates a conserved lysine residue in translation elongation factor P

Published:2010-08-22 Issue:9 Volume:17 Page:1136-1143
ISSN:1545-9993
Container-title:Nature Structural & Molecular Biology
language:en
Short-container-title:Nat Struct Mol Biol

Author:

Yanagisawa Tatsuo,Sumida Tomomi,Ishii Ryohei,Takemoto Chie,Yokoyama Shigeyuki

Publisher

Springer Science and Business Media LLC

Subject

Molecular Biology,Structural Biology

Link

http://www.nature.com/articles/nsmb.1889.pdf

Reference59 articles.

1. Schimmel, P. Aminoacyl tRNA synthetases: general scheme of structure-function relationships in the polypeptides and recognition of transfer RNAs. Annu. Rev. Biochem. 56, 125–158 (1987).

2. Ibba, M. & Söll, D. Aminoacyl-tRNA synthesis. Annu. Rev. Biochem. 69, 617–650 (2000).

3. Eriani, G., Delarue, M., Poch, O., Gangloff, J. & Moras, D. Partition of tRNA synthetases into two classes based on mutually exclusive sets of sequence motifs. Nature 347, 203–206 (1990).

4. Cusack, S., Berthet-Colominas, C., Hartlein, M., Nassar, N. & Leberman, R. A second class of synthetase structure revealed by X-ray analysis of Escherichia coli seryl-tRNA synthetase at 2.5 Å. Nature 347, 249–255 (1990).

5. Roy, H., Becker, H.D., Reinbolt, J. & Kern, D. When contemporary aminoacyl-tRNA synthetases invent their cognate amino acid metabolism. Proc. Natl. Acad. Sci. USA 100, 9837–9842 (2003).

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