Skip to main content
Journal of Bacteriology logoLink to Journal of Bacteriology
. 1990 Jun;172(6):3519–3523. doi: 10.1128/jb.172.6.3519-3523.1990

Characterization of biological ice nuclei from a lichen.

T L Kieft 1, T Ruscetti 1
PMCID: PMC209172  PMID: 2188965

Abstract

Biological ice nuclei (active at approximately -4 degrees C) were extracted from cells of the lichen Rhizoplaca chrysoleuca by sonication. Sensitivity to proteases, guanidine hydrochloride, and urea showed these nuclei to be proteinaceous. The nuclei were relatively heat stable, active from pH 1.5 to 12, and active without lipids, thereby demonstrating significant differences from bacterial ice nuclei.

Full text

PDF
3519

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Corotto L. V., Wolber P. K., Warren G. J. Ice nucleation activity of Pseudomonas fluorescens: mutagenesis, complementation analysis and identification of a gene product. EMBO J. 1986 Feb;5(2):231–236. doi: 10.1002/j.1460-2075.1986.tb04203.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Govindarajan A. G., Lindow S. E. Phospholipid requirement for expression of ice nuclei in Pseudomonas syringae and in vitro. J Biol Chem. 1988 Jul 5;263(19):9333–9338. [PubMed] [Google Scholar]
  3. Govindarajan A. G., Lindow S. E. Size of bacterial ice-nucleation sites measured in situ by radiation inactivation analysis. Proc Natl Acad Sci U S A. 1988 Mar;85(5):1334–1338. doi: 10.1073/pnas.85.5.1334. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Kieft T. L. Ice nucleation activity in lichens. Appl Environ Microbiol. 1988 Jul;54(7):1678–1681. doi: 10.1128/aem.54.7.1678-1681.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Kozloff L. M., 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):845–846. doi: 10.1126/science.226.4676.845. [DOI] [PubMed] [Google Scholar]
  6. Kozloff L. M., Schofield M. A., Lute M. Ice nucleating activity of Pseudomonas syringae and Erwinia herbicola. J Bacteriol. 1983 Jan;153(1):222–231. doi: 10.1128/jb.153.1.222-231.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Lindow S. E., Lahue E., Govindarajan A. G., Panopoulos N. J., Gies D. Localization of ice nucleation activity and the iceC gene product in Pseudomonas syringae and Escherichia coli. Mol Plant Microbe Interact. 1989 Sep-Oct;2(5):262–272. doi: 10.1094/mpmi-2-262. [DOI] [PubMed] [Google Scholar]
  8. Orser C., Staskawicz B. J., Panopoulos N. J., Dahlbeck D., Lindow S. E. Cloning and expression of bacterial ice nucleation genes in Escherichia coli. J Bacteriol. 1985 Oct;164(1):359–366. doi: 10.1128/jb.164.1.359-366.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Phelps P., Giddings T. H., Prochoda M., Fall R. Release of cell-free ice nuclei by Erwinia herbicola. J Bacteriol. 1986 Aug;167(2):496–502. doi: 10.1128/jb.167.2.496-502.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Southworth M. W., Wolber P. K., Warren G. J. Nonlinear relationship between concentration and activity of a bacterial ice nucleation protein. J Biol Chem. 1988 Oct 15;263(29):15211–15216. [PubMed] [Google Scholar]
  11. Wolber P. K., Deininger C. A., Southworth M. W., Vandekerckhove J., van Montagu M., Warren G. J. Identification and purification of a bacterial ice-nucleation protein. Proc Natl Acad Sci U S A. 1986 Oct;83(19):7256–7260. doi: 10.1073/pnas.83.19.7256. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Yang D. S., Sax M., Chakrabartty A., Hew C. L. Crystal structure of an antifreeze polypeptide and its mechanistic implications. Nature. 1988 May 19;333(6170):232–237. doi: 10.1038/333232a0. [DOI] [PubMed] [Google Scholar]

Articles from Journal of Bacteriology are provided here courtesy of American Society for Microbiology (ASM)

RESOURCES