Carboxy-terminal CVLS-sequence-specific protein farnesyltransferase from the eyes of the shrimpPenaeus japonicus: Purification and characterization

✍ Scribed by Wu, Chia-Ssu; Chuang, Nin-Nin

• Publisher: John Wiley and Sons
• Year: 1996
• Tongue: English
• Weight: 872 KB
• Volume: 275
• Category: Article
• ISSN: 0022-104X
• DOI: 10.1002/(sici)1097-010x(19960801)275:5<346::aid-jez3>3.0.co;2-p

✦ Synopsis

Pmtein farnesyltransferase from the eyes of Penaeus japonicus farnesylates predominantly H-ras-specific carboxyl termini, with the sequence CVLS, but not the K-ras-specific sequence CVIM or the protein geranylgeranyltransferase-specific sequence CAIL. The purified protein farnesy1tra.nsferase from shrimp was found by immunoblotting and polyacrylamide gel electrophoresis under denaturing conditions to consist of subunits of Mr 49,000 and Mr 48,000. Since the active pinotein farnesyltransferase was found to have a relative mass of 100,000, the purified enzyme was deduced to be a heterodimer. The enzyme had an optimal pH of 6 and a K, of 14 2 1 pM with the synthetic peptide RTRCVLSH as the substrate. The enzyme was activated by Mn++ and Mg++ but inhibited by Ca++ ions.