Myristoylated proteins and peptidyl myristoyltransferase
Book
·
OSTI ID:6703638
The distribution and intracellular locations of myristoylated proteins have been examined in cultured cells. Incubating a variety of cells in minimal medium containing //sup 3/H/ myristate led to the incorporation of labeled myristate into as many as twenty-five different intracellular proteins. The incorporation increased linearly with time for up to six hours and then increased more slowly for an additional ten hours. The chemical stability indicated that the attachment was covalent and excluded nucleophile-labile bonds such as thioesters. Fluorographs of proteins modified by //sup 3/H/ myristate and resolved on gradient SDS-PAGE showed patterns that differed from cell type to cell type. To examine the intracellular locations of the myristate-labeled proteins, cells were isotonically subfractionated. Most of the myristate-labeled proteins remained in the high speed supernatant devoid of microsomal membranes. This indicated that the myristate modification in itself is not sufficient to serve as an anchor for membrane association. Myristate labeled catalytic subunit of the cyclic AMP dependent protein kinase was specifically immunoprecipitated from an aliquot of the high speed supernatant proteins. However, the prominent tyrosine protein kinase of the murine lymphoma cell line LSTRA, pp56/sup lstra/, also incorporated myristate and was specifically immunoprecipitated from the high speed pellet (particulate) fraction of labeled LSTRA cells. To begin to understand the biochemical mechanism of myristate attachment to protein. The authors partially purified and characterized the peptidyl myristoyltransferase from monkey liver. Recovery of enzymatic activity was 69%.
- OSTI ID:
- 6703638
- Country of Publication:
- United States
- Language:
- English
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Protein N-myristoylation
Journal Article
·
Sat Jul 01 00:00:00 EDT 1989
· Proceedings of the National Academy of Sciences of the United States of America; (USA)
·
OSTI ID:5517145
Functional analysis of protein N-myristoylation: Metabolic labeling studies using three oxygen-substituted analogs of myristic acid and cultured mammalian cells provide evidence for protein-sequence-specific incorporation and analog-specific redistribution
Journal Article
·
Wed Oct 31 23:00:00 EST 1990
· Proceedings of the National Academy of Sciences of the United States of America; (United States)
·
OSTI ID:5603336
Protein N-myristoylation
Thesis/Dissertation
·
Sat Dec 31 23:00:00 EST 1988
·
OSTI ID:5674280
Related Subjects
550201* -- Biochemistry-- Tracer Techniques
59 BASIC BIOLOGICAL SCIENCES
ANIMAL CELLS
ANIMALS
BIOCHEMISTRY
BODY
CARBOXYLIC ACIDS
CELL CULTURES
CHEMISTRY
DIGESTIVE SYSTEM
DISTRIBUTION
ENZYMES
GLANDS
LABELLED COMPOUNDS
LIVER
MAMMALS
MICE
MONKEYS
MONOCARBOXYLIC ACIDS
ORGANIC ACIDS
ORGANIC COMPOUNDS
ORGANS
PRIMATES
PROTEINS
RODENTS
SUBCELLULAR DISTRIBUTION
TETRADECANOIC ACID
TRANSFERASES
TRITIUM COMPOUNDS
TUMOR CELLS
VERTEBRATES
59 BASIC BIOLOGICAL SCIENCES
ANIMAL CELLS
ANIMALS
BIOCHEMISTRY
BODY
CARBOXYLIC ACIDS
CELL CULTURES
CHEMISTRY
DIGESTIVE SYSTEM
DISTRIBUTION
ENZYMES
GLANDS
LABELLED COMPOUNDS
LIVER
MAMMALS
MICE
MONKEYS
MONOCARBOXYLIC ACIDS
ORGANIC ACIDS
ORGANIC COMPOUNDS
ORGANS
PRIMATES
PROTEINS
RODENTS
SUBCELLULAR DISTRIBUTION
TETRADECANOIC ACID
TRANSFERASES
TRITIUM COMPOUNDS
TUMOR CELLS
VERTEBRATES