Glycosylation of yeast aspartyl—tRNA synthetase

FEBS Letters

Colas, Bernard¹  Boulanger, Yves¹ 

[1] Laboratoire de Biochimie, Institut de Biologie Moleculaire et Cellulaire du CNRS, 15, rue René Descartes, 67084 Strasbourg Cédex, France

关键词: Aminoacyl—tRNA synthetase;    Aspartyl—tRNA synthetase;    Glycosylation;    Protein modification;   

DOI  :  10.1016/0014-5793(83)80813-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Several lines of evidence establish that the crystallizable aspartyl—tRNA synthetase from Baker's yeast contains some covalently bound glucose: (i) a positive staining of the enzyme was obtained after polyacrylamide gel electrophoresis followed by the concanavalin A-peroxidase test which is specific for glucose and mannose containing proteins; (ii) thin-layer chromatography and gas-liquid chromatography revealed the presence of glucose in enzyme hydrolysates; (iii) immunoaffinoelectrophoresis in agarose gels containing concanavalin A and antibodies raised against aspartyl—tRNA synthetase showed that the enzyme was able to precipitate entirely in the lectin. Finally incubation of the enzyme with [¹⁴C]glucose or [¹⁴C]glucose 6-phosphate led to the incorporation of radioactivity into trichloroacetic acid-precipitable protein. Indeed immunoprecipitation of [¹⁴C]glucose-labelled aspartyl-tRNA synthetase with specific antibodies using the rocket method followed by autoradiography gave a radioactive peak. This last result also demonstrates the possibility of in vitro glycosylation of yeast aspartyl—tRNA synthetase.

【 授权许可】

Unknown