Formation of an Actin-Like Filament Concurrent with the Enzymatic Synthesis of Inorganic Polyphosphate

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 si...

Full description

Saved in:
Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 2004-11, Vol.101 (45), p.15876-15880
Main Authors: Gómez-García, María R., Kornberg, Arthur
Format: Article
Language:English
Subjects:
Actins
Actins - metabolism
Actins - ultrastructure
Adenosine Triphosphate - metabolism
Amino acids
Animals
Biochemistry
Biological Sciences
Chemical synthesis
Deoxyribonuclease I - pharmacology
Dictyostelium - enzymology
Dictyostelium discoideum
Electron microscopy
Energy Metabolism
Enzymes
Gels
Hydrolysis
Kinetics
Microscopy, Electron
Phalloidine - pharmacology
Phosphates
Phosphotransferases (Phosphate Group Acceptor) - metabolism
Polyphosphates
Polyphosphates - metabolism
Proteins
Salts
Vacuoles
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary: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.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.0406923101