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PMID:15496465
| Citation |
Gómez-García, MR and Kornberg, A (2004) Formation of an actin-like filament concurrent with the enzymatic synthesis of inorganic polyphosphate. Proc. Natl. Acad. Sci. U.S.A. 101:15876-80 |
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| Abstract |
Inorganic polyphosphate (poly P), a chain of hundreds of phosphate residues linked by ATP-like bonds, is found in every cell in nature and is commonly produced from ATP by poly P kinases (e.g., PPK1). Dictyostelium discoideum, the social slime mold, possesses a PPK activity (DdPPK1) with sequence similarity to bacterial PPKs. We find here a previously unrecognized PPK (DdPPK2) in D. discoideum with the sequences and properties of actin-related proteins (Arps) that are similar to muscle actins in size, properties, and globular-filamentous structural transitions. Significantly, the unique actin inhibitors, phalloidin and DNase I, also inhibit synthesis of poly P by DdPPK2. Thus, this particular Arp complex is an enzyme that can polymerize into an actin-like filament concurrent with its synthesis of a poly P chain in a fully reversible reaction. |
| Links |
PubMed PMC528760 Online version:10.1073/pnas.0406923101 |
| Keywords |
Actins/metabolism; Actins/ultrastructure; Adenosine Triphosphate/metabolism; Animals; Deoxyribonuclease I/pharmacology; Dictyostelium/enzymology; Energy Metabolism; Hydrolysis; Kinetics; Microscopy, Electron; Phalloidine/pharmacology; Phosphotransferases (Phosphate Group Acceptor)/metabolism; Polyphosphates/metabolism |
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Significance
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| Gene product | Qualifier | GO ID | GO term name | Evidence Code | with/from | Aspect | Notes | Status |
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