Substrate selection by aminoacyl-tRNA synthetases.

M. Ibba; H. U. Thomann; K. W. Hong; J. M. Sherman; I. Weygand-Durasevic; S. Sever; N. Stange-Thomann; M. Praetorius; D. Söll

Substrate selection by aminoacyl-tRNA synthetases.

M. Ibba
, H. U. Thomann
, K. W. Hong
, J. M. Sherman
, I. Weygand-Durasevic
, S. Sever
, N. Stange-Thomann
, M. Praetorius
, D. Söll

Research output: Contribution to journal › Review article › peer-review

Abstract

The integration of genetic and biochemical approaches to study the crystal structure of the glutaminyl-tRNA synthetase (GlnRS):tRNA(Gln):ATP complex has elucidated the mechanism by which GlnRS selects its cognate tRNA for aminoacylation. Three principal types of interaction have been identified: interaction with specific bases in the cognate tRNA, rejection of non-cognate tRNAs, and activation of the active site upon cognate tRNA binding. The recent solving of the crystal structure of tryptophanyl-tRNA synthetase (TrpRS) has allowed comparable studies to be initiated in an aminoacyl-tRNA synthetase which, unlike GlnRS, does not require tRNA binding prior to amino acid activation.

Original language	English (US)
Pages (from-to)	40-42
Number of pages	3
Journal	Nucleic acids symposium series
Issue number	33
State	Published - 1995
Externally published	Yes

ASJC Scopus subject areas

General Medicine

Cite this

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title = "Substrate selection by aminoacyl-tRNA synthetases.",

abstract = "The integration of genetic and biochemical approaches to study the crystal structure of the glutaminyl-tRNA synthetase (GlnRS):tRNA(Gln):ATP complex has elucidated the mechanism by which GlnRS selects its cognate tRNA for aminoacylation. Three principal types of interaction have been identified: interaction with specific bases in the cognate tRNA, rejection of non-cognate tRNAs, and activation of the active site upon cognate tRNA binding. The recent solving of the crystal structure of tryptophanyl-tRNA synthetase (TrpRS) has allowed comparable studies to be initiated in an aminoacyl-tRNA synthetase which, unlike GlnRS, does not require tRNA binding prior to amino acid activation.",

author = "M. Ibba and Thomann, \{H. U.\} and Hong, \{K. W.\} and Sherman, \{J. M.\} and I. Weygand-Durasevic and S. Sever and N. Stange-Thomann and M. Praetorius and D. S{\"o}ll",

year = "1995",

language = "English (US)",

pages = "40--42",

journal = "Nucleic acids symposium series",

issn = "0261-3166",

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TY - JOUR

T1 - Substrate selection by aminoacyl-tRNA synthetases.

AU - Ibba, M.

AU - Thomann, H. U.

AU - Hong, K. W.

AU - Sherman, J. M.

AU - Weygand-Durasevic, I.

AU - Sever, S.

AU - Stange-Thomann, N.

AU - Praetorius, M.

AU - Söll, D.

PY - 1995

Y1 - 1995

N2 - The integration of genetic and biochemical approaches to study the crystal structure of the glutaminyl-tRNA synthetase (GlnRS):tRNA(Gln):ATP complex has elucidated the mechanism by which GlnRS selects its cognate tRNA for aminoacylation. Three principal types of interaction have been identified: interaction with specific bases in the cognate tRNA, rejection of non-cognate tRNAs, and activation of the active site upon cognate tRNA binding. The recent solving of the crystal structure of tryptophanyl-tRNA synthetase (TrpRS) has allowed comparable studies to be initiated in an aminoacyl-tRNA synthetase which, unlike GlnRS, does not require tRNA binding prior to amino acid activation.

AB - The integration of genetic and biochemical approaches to study the crystal structure of the glutaminyl-tRNA synthetase (GlnRS):tRNA(Gln):ATP complex has elucidated the mechanism by which GlnRS selects its cognate tRNA for aminoacylation. Three principal types of interaction have been identified: interaction with specific bases in the cognate tRNA, rejection of non-cognate tRNAs, and activation of the active site upon cognate tRNA binding. The recent solving of the crystal structure of tryptophanyl-tRNA synthetase (TrpRS) has allowed comparable studies to be initiated in an aminoacyl-tRNA synthetase which, unlike GlnRS, does not require tRNA binding prior to amino acid activation.

UR - https://www.scopus.com/pages/publications/0029448762

UR - https://www.scopus.com/pages/publications/0029448762#tab=citedBy

M3 - Review article

C2 - 8643392

AN - SCOPUS:0029448762

SN - 0261-3166

SP - 40

EP - 42

JO - Nucleic acids symposium series

JF - Nucleic acids symposium series

IS - 33

ER -

Substrate selection by aminoacyl-tRNA synthetases.

Abstract

ASJC Scopus subject areas

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