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

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

Overproduction and domain structure of the glutamyl-tRNA synthetase of Escherichia coli

1989 ◽  
Vol 67 (8) ◽  
pp. 404-410 ◽  
Author(s):  
Anne Brisson ◽  
Yves V. Brun ◽  
Alexander W. Bell ◽  
Paul H. Roy ◽  
Jacques Lapointe
Keyword(s):  
Escherichia Coli ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Domain Structure ◽  
Sequence Similarity ◽  
Trna Synthetase ◽  
Amino Acid Sequence Similarity ◽  
Structural Domains ◽  
E Coli ◽  
Domain Structures

The charging of glutamate on tRNAGlu is catalyzed by glutamyl-tRNA synthetase, a monomer of 53.8 kilodaltons in Escherichia coli. To obtain the large amounts of enzyme necessary for the identification of structural domains, we have inserted the structural gene gltX in the conditional runaway-replication plasmid pOU61, which led to a 350-fold overproduction of glutamyl-tRNA synthetase. Partial proteolysis of this enzyme revealed the existence of preferential sites of attack that, according to their N-terminal sequences, delimit regions of 12.9, 2.3, 12.1, and 26.5 kilodaltons from the N- to C-terminal of the enzyme. Their sizes suggest that the 2.3-kilodalton fragment is a hinge structure, and that those of 12.9, 12.1, and 26.5 kilodaltons are domain structures. The 12.9-kilodalton domain of the glutamyl-tRNA synthetase of E. coli is the only long region of this enzyme displaying a good amino acid sequence similarity with the glutaminyl-tRNA synthetase of Escherichia coli.Key words: glutamyl-tRNA synthetase, structural domains, overproduction, runaway-replication plasmid, Escherichia coli.

scholarly journals Cloning of the Glutamyl-tRNA Synthetase (gltX) Gene from Pseudomonas aeruginosa

1999 ◽  
Vol 181 (11) ◽  
pp. 3582-3586 ◽  
Author(s):  
Clifton V. Franklund ◽  
Joanna B. Goldberg
Keyword(s):  
Escherichia Coli ◽  
Pseudomonas Aeruginosa ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Rhizobium Meliloti ◽  
Trna Synthetase ◽  
Temperature Sensitive

ABSTRACT The glutamyl-tRNA synthetase (gltX) gene fromPseudomonas aeruginosa was identified. A plasmid containing a 2.3-kb insert complemented the temperature-sensitive gltXmutation of Escherichia coli JP1449, and GltX activity was demonstrated. The inferred amino acid sequence of this gene showed 50.6% identity with GltX from Rhizobium meliloti.

scholarly journals Derived amino acid sequence and identification of active site residues of Escherichia coli beta-hydroxydecanoyl thioester dehydrase.

1988 ◽  
Vol 263 (10) ◽  
pp. 4641-4646 ◽  
Author(s):  
J E Cronan ◽  
W B Li ◽  
R Coleman ◽  
M Narasimhan ◽  
D de Mendoza ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Active Site ◽  
Active Site Residues

scholarly journals The Amino Acid Sequence of the A Protein (α Subunit) of the Tryptophan Synthetase of Escherichia coli

1967 ◽  
Vol 242 (22) ◽  
pp. 5442-5446 ◽  
Author(s):  
John R. Guest ◽  
Gabriel R. Drapeau ◽  
Bruce C. Carlton ◽  
Charles Yanofsky
Keyword(s):  
Escherichia Coli ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Α Subunit ◽  
Tryptophan Synthetase

scholarly journals Nucleotide sequence of the melB gene and characteristics of deduced amino acid sequence of the melibiose carrier in Escherichia coli.

1984 ◽  
Vol 259 (7) ◽  
pp. 4320-4326 ◽  
Author(s):  
H Yazyu ◽  
S Shiota-Niiya ◽  
T Shimamoto ◽  
H Kanazawa ◽  
M Futai ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Amino Acid ◽  
Nucleotide Sequence ◽  
Amino Acid Sequence
Sign in / Sign up

Export Citation Format

Share Document