Domains of the Escherichia coli threonyl-tRNA synthetase translational operator and their relation to threonine tRNA isoacceptors

C. Brunel; J. Caillet; P. Lesage; M. Graffe; J. Dondon; H. Moine; P. Romby; C. Ehresmann; B. Ehresmann; M. Grunberg-Manago; M. Springer

doi:10.1016/0022-2836(92)90212-3

Domains of the Escherichia coli threonyl-tRNA synthetase translational operator and their relation to threonine tRNA isoacceptors

Journal of Molecular Biology ◽

10.1016/0022-2836(92)90212-3 ◽

1992 ◽

Vol 227 (3) ◽

pp. 621-634 ◽

Cited By ~ 20

Author(s):

C. Brunel ◽

J. Caillet ◽

P. Lesage ◽

M. Graffe ◽

J. Dondon ◽

...

Keyword(s):

Escherichia Coli ◽

Trna Synthetase ◽

Translational Operator ◽

Trna Isoacceptors

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A Novel Approach to Introduce Site-Directed Specific Cross-Links Within RNA-Protein Complexes. Application to the Escherichia Coli Threonyl-tRNA Synthetase/Translational Operator Complex

European Journal of Biochemistry ◽

10.1111/j.1432-1033.1995.0726d.x ◽

1995 ◽

Vol 231 (3) ◽

pp. 726-735 ◽

Cited By ~ 15

Author(s):

Marina Zenkova ◽

Chantal Ehresmann ◽

Joel Caillet ◽

Mathias Springer ◽

Galina Karpova ◽

...

Keyword(s):

Escherichia Coli ◽

Protein Complexes ◽

Trna Synthetase ◽

Novel Approach ◽

Translational Operator ◽

Cross Links ◽

Rna Protein Complexes

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Secondary structure of the Escherichia coli translational operator of threonyl-tRNA synthetase and relationship to its function

Gene ◽

10.1016/0378-1119(88)90142-4 ◽

1988 ◽

Vol 72 (1-2) ◽

pp. 187-188

Author(s):

Bernard Ehresmann ◽

Hervé Moine ◽

Pascale Romby ◽

Mathias Springer ◽

Marianne Grunberg-Manago ◽

...

Keyword(s):

Escherichia Coli ◽

Secondary Structure ◽

Trna Synthetase ◽

Translational Operator

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Faculty Opinions recommendation of A conserved threonine within Escherichia coli leucyl-tRNA synthetase prevents hydrolytic editing of leucyl-tRNALeu.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.1000366.1351 ◽

2001 ◽

Author(s):

Anne-Catherine Dock-Bregeon

Keyword(s):

Escherichia Coli ◽

Trna Synthetase

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Faculty Opinions recommendation of Discrimination of tRNA(Leu) isoacceptors by the mutants of Escherichia coli leucyl-tRNA synthetase in editing.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.1009103.118807 ◽

2002 ◽

Author(s):

Anne-Catherine Dock-Bregeon

Keyword(s):

Escherichia Coli ◽

Trna Synthetase

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The catalytic mechanism of the glutamyl-tRNA synthetase from Escherichia coli. Detection of an intermediate complex in which glutamate is activated.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(19)85976-8 ◽

1980 ◽

Vol 255 (5) ◽

pp. 1956-1961

Author(s):

D. Kern ◽

J. Lapointe

Keyword(s):

Escherichia Coli ◽

Catalytic Mechanism ◽

Trna Synthetase ◽

Intermediate Complex

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Purification and properties of alanine tRNA synthetase from Escherichia coli A tetramer of identical subunits.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(19)70119-7 ◽

1981 ◽

Vol 256 (1) ◽

pp. 198-204 ◽

Cited By ~ 2

Author(s):

S.D. Putney ◽

R.T. Sauer ◽

P.R. Schimmel

Keyword(s):

Escherichia Coli ◽

Trna Synthetase ◽

Purification And Properties

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31P NMR of the reversible methionine activation reaction catalyzed by methionyl-tRNA synthetase of Escherichia coli. Equilibrium, interconversion rates, and NMR parameters of the enzyme-bound species.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(19)70624-3 ◽

1980 ◽

Vol 255 (17) ◽

pp. 8164-8169

Author(s):

G. Fayat ◽

S. Blanquet ◽

B.D. Nageswara Rao ◽

M. Cohn

Keyword(s):

Escherichia Coli ◽

31P Nmr ◽

Trna Synthetase ◽

Activation Reaction ◽

Nmr Parameters ◽

Methionyl Trna Synthetase

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Nucleotide and deduced amino acid sequence of human threonyl-tRNA synthetase reveals extensive homology to the Escherichia coli and yeast enzymes

Journal of Biological Chemistry ◽

10.1016/s0021-9258(18)92906-6 ◽

1991 ◽

Vol 266 (15) ◽

pp. 9919-9923

Author(s):

M.E. Cruzen ◽

S.M. Arfin

Keyword(s):

Escherichia Coli ◽

Amino Acid ◽

Amino Acid Sequence ◽

Trna Synthetase

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Studies on arginyl-tRNA synthetase from Escherichia coli B. Dual role of metals in enzyme catalysis.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(17)33951-0 ◽

1976 ◽

Vol 251 (1) ◽

pp. 241-246

Author(s):

J E Craine ◽

A Peterkofsky

Keyword(s):

Escherichia Coli ◽

Enzyme Catalysis ◽

Trna Synthetase ◽

Dual Role ◽

Escherichia Coli B

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Cotranscription of the Escherichia coli isoleucyl-tRNA synthetase (ileS) and prolipoprotein signal peptidase (lsp) genes. Fine-structure mapping of the lsp internal promoter.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(19)75939-0 ◽

1987 ◽

Vol 262 (1) ◽

pp. 389-393

Author(s):

K W Miller ◽

H C Wu

Keyword(s):

Escherichia Coli ◽

Fine Structure ◽

Trna Synthetase ◽

Signal Peptidase ◽

Structure Mapping ◽

Internal Promoter

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