Abstract
Barley chloroplast glutamate-tRNA ligase was purified using salicylate-Sepharose and phosphocellulose chromatography. The purified enzyme amino-acylates δ-ALA-RNA, the other glutamate acceptor tRNAs of the chloroplast, as well as E. coli tRNA 2 Glu . An antibody was raised against the purified ligase and coupled to Sepharose. The enzyme purified by immunoaffinity chromatography has a subunit molecular weight of 54 kilodaltons. The dehydrogenase involved in δ-aminolevulinate synthesis was separated from the ligase by immunoaffinity chromatography. Reconstitution experiments confirmed that glutamate-tRNA ligase participates in δ-aminolevulinate synthesis and it is suggested that a single glutamate-tRNA ligase provides activated glutamate for both chlorophyll and protein biosynthesis. An antibody raised against B. subtilis glutamate-tRNA ligase cross reacted with the barley glutamate-tRNA ligase.
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