Two isomorphous heavy-atom derivatives of crystalline methionyl-tRNA synthetase from Escherichia coli
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Two isomorphous heavy-atom derivatives of crystalline methionyl-tRNA synthetase from Escherichia coli.
Aminoacyl-tRNA synthetases play a key role in the biosynthesis of proteins by their ability to specifically recognize an amino acid and its corresponding tRNA. An understanding of the basis of such specific proteinnucleic acid recognition requires the knowledge of the structure of the molecules involved. This goal is probably not very remote now since a high resolution model of yeast phenylalan...
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Respiratory deficient mutants of Saccharomyces cerevisiae previously assigned to complementation group G59 are pleiotropically deficient in respiratory chain components and in mitochondrial ATPase. This phenotype has been shown to be a consequence of mutations in a nuclear gene coding for mitochondrial leucyl-tRNA synthetase. The structural gene (MSL1) coding for the mitochondrial enzyme has be...
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The metS gene encoding homodimeric methionyl-tRNA synthetase from Bacillus stearothermophilus has been cloned and a 2880 base pair sequence solved. Comparison of the deduced enzyme protomer sequence (Mr 74,355) with that of the E. coli methionyl-tRNA synthetase protomer (Mr 76,124) revealed a relatively low level (32%) of identities, although both enzymes have very similar biochemical propertie...
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Methionyl-tRNA synthetase (MetRS) belongs to the family of 20 enzymes essential for protein biosynthesis. It links covalently methionine with its cognate tRNA. Crystal structures solved for bacterial MetRSs have given a number of interesting insights into enzyme architecture and methionylation catalysis. A comparison of sequences of MetRSs belonging to all kingdoms of life, as well as numerous ...
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Methionyl-tRNA synthetase has been purified from a yeast strain carrying the MESl structural gene on a high copy number plasmid (pFL1). The purified enzyme is a monomer of M, = 85,000 in contrast to its counterpart from Escherichia coli which is a dimer made up of identical subunits (M, = 76,000; Dardel, F., Fayat, G., and Blanquet, S . (1984) J. Bucteriol. 160,1115-1122). The yeast enzyme was ...
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ژورنال
عنوان ژورنال: FEBS Letters
سال: 1974
ISSN: 0014-5793
DOI: 10.1016/0014-5793(74)80344-3