Acylation of proteins with myristic acid occurs cotranslationally

Journal Article · Fri Nov 27 04:00:00 EST 1987 · Science (Washington, D.C.); (United States)

DOI:https://doi.org/10.1126/science.3685978· OSTI ID:5607811

Wilcox, C; Hu, J S; Olson, E N

Several proteins of viral and cellular origin are acylated with myristic acid early during their biogenesis. To investigate the possibility that myristylation occurred cotranslationally, the BC/sup 3/H1 muscle cell line, which contains a broad array of myristylated proteins, was pulse-labeled with (/sup 3/H)myristic acid. Nascent polypeptide chains covalently associated with transfer RNA were isolated subsequently by ion-exchange chromatography. (/sup 3/H)Myristate was attached to nascent chains through an amide linkage and was identified by thin-layer chromatography after its release from nascent chains by acid methanolysis. Inhibition of cellular protein synthesis with puromycin resulted in cessation of (/sup 3/H)myristate-labeling of nascent chains, in agreement with the dependence of this modification on protein synthesis in vivo. These data represent a direct demonstration that myristylation of proteins is a cotranslational modification.

• Research Organization: Univ. of Texas, M.D. Anderson Hospital and Tumor Institute, Houston
• OSTI ID: 5607811
• Journal Information: Science (Washington, D.C.); (United States), Journal Name: Science (Washington, D.C.); (United States) Vol. 238:4831; ISSN SCIEA
• Country of Publication: United States
• Language: English

Related Subjects

550201* -- Biochemistry-- Tracer Techniques
59 BASIC BIOLOGICAL SCIENCES
ACYLATION
AMINO ACIDS
CARBOXYLIC ACIDS
CHEMICAL REACTIONS
CHROMATOGRAPHY
DRUGS
ION EXCHANGE CHROMATOGRAPHY
LABELLED COMPOUNDS
LIPOTROPIC FACTORS
METHIONINE
MONOCARBOXYLIC ACIDS
MUSCLES
ORGANIC ACIDS
ORGANIC COMPOUNDS
ORGANIC SULFUR COMPOUNDS
PROTEINS
SEPARATION PROCESSES
STRUCTURE-ACTIVITY RELATIONSHIPS
TETRADECANOIC ACID
THIN-LAYER CHROMATOGRAPHY
TRITIUM COMPOUNDS