Evidence for N-Terminal Myristoylation of Tetrahymena Arginine Kinase Using Peptide Mass Fingerprinting Analysis

• Published in: Protein Journal Vol. 35; no. 3; pp. 212 - 217
• Main Authors: Motomura, Shou, Suzuki, Tomohiko
• Format: Journal Article
• Language: English
• Published: New York Springer US 01.06.2016; Springer; Springer Nature B.V
• Subjects: Amino Acid Sequence; Analysis; Animal Anatomy; Arginine; Arginine Kinase - chemistry; Biochemistry; Bioorganic Chemistry; Chemistry; Chemistry and Materials Science; Enzymes; Fatty acids; Histology; Kinases; Morphology; Myristic Acid - analysis; Organic Chemistry; Peptides; Peptides - chemistry; Protein biosynthesis; Protein synthesis; Protozoan enzymes; Tetrahymena; Tetrahymena pyriformis; Tetrahymena pyriformis - chemistry; Tetrahymena pyriformis - cytology; Tetrahymena pyriformis - enzymology; Peptide mass fingerprinting; Myristoylation; Arginine kinase; Subcellular localization; Tetrahymena pyriformis

In this study, we confirmed N-terminal myristoylation of Tetrahymena pyriformis arginine kinase (AK1) by identifying a myristoylation signal sequence at the N-terminus. A sufficient amount of modified enzyme was synthesized using an insect cell-free protein synthesis system that contains all of the...