Purification and partial amino acid sequence of a glutamyl-tRNA synthetase from Rhizobium meliloti.
A glutamyl-tRNA synthetase has been purified to homogeneity from Rhizobium meliloti, using reversed-phase chromatography as the last step. Amino acid sequencing of the amino-terminal region of the enzyme indicates that it contains a single polypeptide, whose molecular weight is about 54,000, as judged by SDS-gel electrophoresis. The primary structures of the amino-terminus region and of an internal peptide obtained by cleavage of the enzyme with CNBr have similarities of 58 and 48% with regions of the glutamyl-tRNA synthase of Escherichia coli; these are thought to be involved in the binding of ATP and tRNA, respectively. The small amount of glutamyl-tRNA synthetase present in R. meliloti is consistent with the metabolic regulation of the biosynthesis of many aminoacyl-tRNA synthetases.
Laberge
S
S
Département de biochimie, Faculté des sciences et de génie, Université Laval, Québec, Canada.
Belair
M
M
Verreault
A
A
Bell
A W
AW
Bordeleau
L M
LM
Lapointe
J
J
D000595:Amino Acid Sequence; D000604:Amino Acyl-tRNA Synthetases / Q000302:isolation & purification; D001426:Bacterial Proteins / Q000032:analysis; D002455:Cell Division; D002846:Chromatography, Affinity; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D002853:Chromatography, Liquid; D003488:Cyanogen Bromide; D005975:Glutamate-tRNA Ligase / Q000302:isolation & purification; D008969:Molecular Sequence Data; D012231:Rhizobium / Q000201:enzymology*; D013045:Species Specificity
D001426:Bacterial Proteins; D000604:Amino Acyl-tRNA Synthetases; D005975:Glutamate-tRNA Ligase; D003488:Cyanogen Bromide