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Kozloff LM, Lute M, Westaway D. Phosphatidylinositol as a Component of the Ice Nucleating Site of Pseudomonas syringae and Erwinia herbiola. Science. 1984;226(4676):845-6doi: 10.1126/science.226.4676.845.
Kozloff, L. M., Lute, M., & Westaway, D. (1984). Phosphatidylinositol as a Component of the Ice Nucleating Site of Pseudomonas syringae and Erwinia herbiola. Science (New York, N.Y.), 226(4676), 845-6. https://doi.org/10.1126/science.226.4676.845
Kozloff, L M, et al. "Phosphatidylinositol as a Component of the Ice Nucleating Site of Pseudomonas syringae and Erwinia herbiola." Science (New York, N.Y.) vol. 226,4676 (1984): 845-6. doi: https://doi.org/10.1126/science.226.4676.845
Kozloff LM, Lute M, Westaway D. Phosphatidylinositol as a Component of the Ice Nucleating Site of Pseudomonas syringae and Erwinia herbiola. Science. 1984 Nov 16;226(4676):845-6. doi: 10.1126/science.226.4676.845. PMID: 17759892.
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Science. 1984 Nov 16;226(4676):845-6. doi: 10.1126/science.226.4676.845.

Phosphatidylinositol as a Component of the Ice Nucleating Site of Pseudomonas syringae and Erwinia herbiola.

Science (New York, N.Y.)

L M Kozloff, M Lute, D Westaway

PMID: 17759892 DOI: 10.1126/science.226.4676.845

Abstract

Phosphatidylinositol has been identified as a major component of the ice nucleating site on the outer surface of two bacteria, Pseudomonas syringae and Erwinia herbicola. Plant lectins binding to inositol and a highly purified phosphatidylinositol-specific hydrolase (a C(II) lipase) inhibited or decreased the efficiency of the ice nucleating activity (INA) of both bacteria. Extracts of these two INA(+) bacteria had phosphatidylinositol synthase activity while extracts from related INA(-) Pseudomonas or Erwinia strains had no detectable synthase activity. An Escherichia coli strain acquired phosphatidylinositol synthase activity when transformed to the INA(+) phenotype with recombinant plasmids containing fragments of P. syringae DNA.

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