The valyl-tRNA synthetase from Bacillus stearothermophilus has considerable sequence homology with the isoleucyl-tRNA synthetase from Escherichia coli

Biochemistry ◽  
1987 ◽  
Vol 26 (9) ◽  
pp. 2480-2486 ◽  
Author(s):  
Thor J. Borgford ◽  
Nigel J. Brand ◽  
Tamara E. Gray ◽  
Alan R. Fersht
Keyword(s):  
Escherichia Coli ◽  
Sequence Homology ◽  
Bacillus Stearothermophilus ◽  
Trna Synthetase

scholarly journals A comparison of purified valyl-transfer ribonucleic acid synthetase from Bacillus stearothermophilus and from Escherichia coli

1974 ◽  
Vol 139 (2) ◽  
pp. 391-398 ◽  
Author(s):  
Susan Wilkinson ◽  
Jeremy R. Knowles
Keyword(s):  
Escherichia Coli ◽  
Gel Electrophoresis ◽  
Bacillus Stearothermophilus ◽  
Polyacrylamide Gel Electrophoresis ◽  
Gel Filtration ◽  
Binding Constants ◽  
Trna Synthetase ◽  
Subunit Structure ◽  
Filtration Method ◽  
E Coli

The purification of valyl-tRNA synthetase from Bacillus stearothermophilus is described. The protein was greater than 90% homogeneous on polyacrylamide-gel electrophoresis after more than 850-fold purification. It has a molecular weight of 110000, and no evidence was found for the presence of subunit structure. The properties of the purified enzyme were compared with those of purified valyl-tRNA synthetase from Escherichia coli. The thermal stability, pH-stability and dependence of activity on the temperature and pH of the assay are reported. The two enzymes recognize and charge tRNAVal from crude tRNA of the mesophile E. coli and of the thermophile B. stearothermophilus, indiscriminately. The gel-filtration method was extended to measure the binding of tRNA to synthetase directly. Binding constants for tRNAVal to valyl-tRNA synthetase from B. stearothermophilus were determined between 5° and 60°C.

scholarly journals Adenosine triphosphate consumption by bacterial arginyl-transfer ribonucleic acid synthetases

1979 ◽  
Vol 179 (2) ◽  
pp. 407-412 ◽  
Author(s):  
J M Godeau ◽  
J Charlier
Keyword(s):  
Escherichia Coli ◽  
Adenosine Triphosphate ◽  
Ribonucleic Acid ◽  
Adenosine Triphosphatase ◽  
Bacillus Stearothermophilus ◽  
Trna Synthetase ◽  
Luciferase Assay ◽  
Trna Synthetases ◽  
E Coli ◽  
Firefly Luciferin

ATP consumption by arginyl-tRNA synthetases from Escherichia coli and Bacillus stearothermophilus has been investigated by the firefly luciferin–luciferase assay. Arginyl-tRNA synthetase from E. coli utilizes ATP only for aminocylation of tRNA with a 1:1 stoicheiometry. In contrast, we have shown an adenosine triphosphatase activity of arginyl-tRNA synthetase from B. stearothermophilus in the absence of tRNAArg. Dowex chromatography revealed the formation of ADP by the thermophile enzyme; under aminoacylation conditions, AMP was also formed in amounts stoicheiometric with arginyl-tRNA formation.

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