Membrane attachment activates dnaA protein, the initiation protein of chromosome replication in Escherichia coli
ADP and ATP are tightly bound to dnaA protein and are crucial to its function in DNA replication; the exchange of these nucleotides is effected specifically by the acidic phospholipids (cardiolipin and phosphatidylglycerol) present in Escherichia coli membranes. We now find that phospholipids derived from membranes lacking an unsaturated fatty acid (e.g., oleic acid) are unable to promote the exchange. This observation correlates strikingly with the long-known effect of 3-decynoyl-N-acetylcysteamine, a ''suicide analog'' that prevents initiation of a cycle of replication in E. coli by inhibiting the synthesis of oleic acid, an inhibition that can be overcome by providing the cells with oleic acid. Profound influences on the specific binding of dnaA protein to phospholipids by temperature, the content of unsaturated fatty acids, and the inclusion of cholesterol can be explained by the need for the phospholipids to be in fluid-phase vesicles. These findings suggest that membrane attachment of dnaA protein is vital for its function in the initiation of chromosome replication in E. coli.
- Research Organization:
- Stanford Univ. School of Medicine, CA (USA)
- OSTI ID:
- 6584075
- Journal Information:
- Proc. Natl. Acad. Sci. U.S.A.; (United States), Vol. 85:19
- Country of Publication:
- United States
- Language:
- English
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Related Subjects
ESCHERICHIA COLI
DNA REPLICATION
MEMBRANE PROTEINS
BIOLOGICAL FUNCTIONS
ADP
ATP
CELL MEMBRANES
CHOLESTEROL
OLEIC ACID
BACTERIA
CARBOXYLIC ACIDS
CELL CONSTITUENTS
FUNCTIONS
HYDROXY COMPOUNDS
MEMBRANES
MICROORGANISMS
MONOCARBOXYLIC ACIDS
NUCLEIC ACID REPLICATION
NUCLEOTIDES
ORGANIC ACIDS
ORGANIC COMPOUNDS
PROTEINS
STEROIDS
STEROLS
550200* - Biochemistry