Inorganic polyphosphate: a molecule of many functions.
Pursuit of the enzymes that make and degrade polyP has provided analytic reagents which confirm the ubiquity of polyP in microbes and animals and provide reliable means for measuring very low concentrations. Many distinctive functions appear likely for polyP depending on its abundance, chain length, biologic source and subcellular location: an energy supply and ATP substitute, a reservoir for Pi, a chelator of metals, a buffer against alkali, a channel for DNA entry, a cell capsule, and, of major interest, a regulator of responses to stresses and adjustments for survival in the stationary phase of culture growth and development. Whether microbe or human, we depend on adaptations in the stationary phase, a dynamic phase of life. Much attention has focused on the early and reproductive phases of organisms, rather brief intervals of rapid growth, but more concern needs to be given to the extensive period of maturity. Survival of microbial species depends on being able to manage in the stationary phase. In view of the universality and complexity of basic biochemical mechanisms, it would be surprising if some of the variety of polyP functions observed in microorganisms did not apply to aspects of human growth and development, to aging and to the aberrations of disease. Of theoretical interest regarding polyP is its antiquity in prebiotic evolution, which, along with its high energy and phosphate content, make it a plausible precursor to RNA, DNA and proteins. Of practical interest is its many industrial applications, among which is its use in the microbial depollution of Pi in marine environments.
Kornberg
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Department of Biochemistry, Stanford University School of Medicine, California 94305-5307, USA.
D000595:Amino Acid Sequence; D000818:Animals; D006801:Humans; D043564:Inorganic Pyrophosphatase; D008969:Molecular Sequence Data; D011755:Pyrophosphatases
D011755:Pyrophosphatases; D043564:Inorganic Pyrophosphatase