Post-translational arginylation of calreticulin: a new isospecies of calreticulin component of stress granules.

M. B. DECCA, M. A. CARPIO, C. BOSC, M. R. GALIANO, D. JOB, A. ANDRIEUX AND M. E. HALLAK

Journal Biological Chemistry

Año: 2007 vol. 282 p. 8237 - 8237

0021-9258

font face="WarnockPro-Semibold" size="2"> Post-translational arginylation consists of the covalent union of an arginine residue to a Glu, Asp, or Cys amino acid at the N-terminal position of proteins. This reaction is catalyzed by the enzyme arginyl-tRNA protein transferase. Using mass spectrometry, we have recently demonstrated in vitro the post-translational incorporation of arginine into the calcium-binding protein calreticulin (CRT). To further study arginylated CRT we raised an antibody against the peptide (RDPAIYFK) that contains an arginine followed by the first 7 N-terminal amino acids of mature rat CRT. This antibody specifically recognizes CRT obtained from