PMID:6756915
| Citation |
Barker, DG, Ebel, JP, Jakes, R and Bruton, CJ (1982) Methionyl-tRNA synthetase from Escherichia coli. Primary structure of the active crystallised tryptic fragment. Eur. J. Biochem. 127:449-57 |
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| Abstract |
A 3300-base segment of Escherichia coli chromosomal DNA, cloned into pBR322, will complement a methionine auxotroph in which the lesion is a defective methionyl-tRNA synthetase with a much reduced affinity for methionine. Crude extracts of these transformants contain elevated levels of a protein which has a subunit molecular weight of 66 000, methionyl-tRNA synthetase aminoacylation activity in vitro and which cross-reacts with anti-(methionyl-tRNA synthetase) antibodies. This polypeptide is very slightly larger than the well-characterised and crystallised tryptic fragment of methionyl-tRNA synthetase. A DNA sequence of 1750 residues at one end of the cloned insert codes for a non-terminated open reading frame in which we can locate a large number of methionyl-tRNA synthetase tryptic and chymotryptic peptides. We have also sequenced 300 nucleotides upstream of this coding segment where we find a large invert repeat in the putative methionyl-tRNA synthetase promoter region. |
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| Keywords |
Amino Acid Sequence; Amino Acyl-tRNA Synthetases/isolation & purification; Bacterial Proteins/isolation & purification; Chemical Phenomena; Chemistry; Chymotrypsin; Cloning, Molecular; Crystallization; DNA, Bacterial/isolation & purification; Escherichia coli/enzymology; Methionine-tRNA Ligase/genetics; Methionine-tRNA Ligase/isolation & purification; Peptide Fragments/isolation & purification; Trypsin |
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