PMID:2014166
| Citation |
Eriani, G, Dirheimer, G and Gangloff, J (1991) Cysteinyl-tRNA synthetase: determination of the last E. coli aminoacyl-tRNA synthetase primary structure. Nucleic Acids Res. 19:265-9 |
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| Abstract |
The gene coding for E. coli cysteinyl-tRNA synthetase (cysS) was isolated by complementation of a strain deficient in cysteinyl-tRNA synthetase activity at high temperature (43 degrees C). Sequencing of a 2.1 kbp DNA fragment revealed an open reading frame of 1383 bp coding for a protein of 461 amino acid residues with a Mr of 52,280, a value in close agreement with that observed for the purified protein, which behaves as a monomer. The sequence of CysRS bears the canonical His-Ile- Gly -His (HIGH) and Lys-Met-Ser-Lys-Ser (KMSKS) motifs characteristic of the group of enzymes containing a Rossmann fold; furthermore, it shows striking homologies with MetRS (an homodimer of 677 residues) and to a lesser extent with Ile-, Leu-, and ValRS (monomers of 939, 860, and 951 residues respectively). With its monomeric state and smaller size, CysRS is probably more closely related to the primordial aminoacyl-tRNA synthetase from which all have diverged. |
| Links | |
| Keywords |
Amino Acid Sequence; Amino Acyl-tRNA Synthetases/genetics; Codon; Electrophoresis, Polyacrylamide Gel; Escherichia coli/enzymology; Kinetics; Molecular Sequence Data; Sequence Alignment; Sequence Homology, Nucleic Acid; Transcription, Genetic |
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