-
- Michael R. W. Brown
- Department of Biochemistry, Stanford University School of Medicine, Stanford, CA 94305-5307
-
- Arthur Kornberg
- Department of Biochemistry, Stanford University School of Medicine, Stanford, CA 94305-5307
書誌事項
- 公開日
- 2004-11
- DOI
-
- 10.1073/pnas.0406909101
- 公開者
- Proceedings of the National Academy of Sciences
この論文をさがす
説明
<jats:p> Inorganic polyphosphate (poly P), in chains of tens to hundreds of phosphate residues, linked by high-energy bonds, is environmentally ubiquitous and abundant. In prebiotic evolution it could have provided a flexible, polyanionic scaffold to assemble macromolecules. It has been conserved in every cell in nature. In prokaryotes, a major poly P synthetic enzyme is poly P kinase 1 (PPK1), which is found in 100 bacterial genomes, including numerous pathogens. Null mutants of PPK1, with low poly P levels, are defective in survival: namely, they show defective responses to physical/chemical stresses and predation. Pathogens with a PPK1 deletion are defective in biofilm formation, quorum sensing, general stress and stringent responses, motility, and other virulence properties. With the exception of <jats:italic>Dictyostelium</jats:italic> , PPK1 is absent in eukaryotes and provides a novel target for chemotherapy that would affect both virulence and susceptibility to antibacterial compounds. Remarkably, another PPK in <jats:italic>Dictyostelium discoideum</jats:italic> (PPK2) is an actin-related protein (Arp) complex that is polymerized into an actin-like filament, concurrent with its reversible synthesis of a poly P chain from ATP. </jats:p>
収録刊行物
-
- Proceedings of the National Academy of Sciences
-
Proceedings of the National Academy of Sciences 101 (46), 16085-16087, 2004-11
Proceedings of the National Academy of Sciences
