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 [Sekimizu, K. & Kornberg, A. (1988...
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Published in | Proceedings of the National Academy of Sciences - PNAS Vol. 85; no. 19; pp. 7202 - 7205 |
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Main Authors | , |
Format | Journal Article |
Language | English |
Published |
United States
National Academy of Sciences of the United States of America
01.10.1988
National Acad Sciences |
Subjects | |
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Abstract | 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 [Sekimizu, K. & Kornberg, A. (1988) J. Biol. Chem. 263, 7131-7135]. 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. |
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AbstractList | 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. The authors 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. 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 [Sekimizu, K. & Kornberg, A. (1988) J. Biol. Chem. 263, 7131-7135]. 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. 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 [Sekimizu, K. & Kornberg, A. (1988) J. Biol. Chem. 263, 7131-7135]. 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. |
Author | Yung, Benjamin Yat-Ming Kornberg, Arthur |
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Snippet | 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... 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... |
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SubjectTerms | Adenosine Triphosphate - metabolism Bacterial Proteins - metabolism Biochemistry Cardiolipins Cholesterol - pharmacology Cholesterols Chromosomes Cysteamine - analogs & derivatives Cysteamine - pharmacology DNA DNA Replication DNA, Bacterial - biosynthesis DnaA protein Escherichia coli Escherichia coli - genetics Fatty acids Fatty Acids, Unsaturated - analysis inner membranes Membrane Fluidity Oleic Acid Oleic Acids - pharmacology P branes Phospholipids Temperature Unsaturated fatty acids |
Title | Membrane Attachment Activates dnaA Protein, the Initiation Protein of Chromosome Replication in Escherichia coli |
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