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

Bernard Ehresmann; Hervé Moine; Pascale Romby; Mathias Springer; Marianne Grunberg-Manago; Jean-Pierre Ebel; Chantal Ehresmann

doi:10.1016/0378-1119(88)90142-4

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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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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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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An RNA Secondary Structure Switch between the Inactive and Active Conformations of the Escherichia coli 30 S Ribosomal Subunit

Journal of Biological Chemistry ◽

10.1016/s0021-9258(17)31292-9 ◽

1989 ◽

Vol 264 (1) ◽

pp. 540-545

Author(s):

G Ericson ◽

P Wollenzien

Keyword(s):

Escherichia Coli ◽

Secondary Structure ◽

Rna Secondary Structure ◽

Ribosomal Subunit

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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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Effect of the relative position of the UGA codon to the unique secondary structure in the fdhF mRNA on its decoding by selenocysteinyl tRNA in Escherichia coli.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(19)49436-2 ◽

1993 ◽

Vol 268 (31) ◽

pp. 23128-23131

Author(s):

G.F. Chen ◽

L Fang ◽

M Inouye

Keyword(s):

Escherichia Coli ◽

Secondary Structure ◽

Relative Position ◽

Uga Codon

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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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