Molecular organisation of the ice nucleation protein InaV from Pseudomonas syringae

FEBS Lett. 1997 Sep 15;414(3):590-4. doi: 10.1016/s0014-5793(97)01079-x.

Abstract

A new ice nucleation gene from Pseudomonas syringae was isolated and overexpressed as a fully active protein in Escherichia coli in order to gain experimental data about the structure of ice nucleation proteins. No evidence of a signal sequence or secondary glycosylation was found. Differences in the extent of aggregation were shown to modulate the ice nucleation activity. The circular dichroism spectrum of the purified protein indicated the presence of beta-sheet structure. This finding supports a recently proposed hypothetical model for the structure of ice nucleation proteins, which provides a plausible explanation for their aggregation tendency.

Publication types

  • Comparative Study

MeSH terms

  • Bacterial Outer Membrane Proteins / chemistry*
  • Bacterial Outer Membrane Proteins / genetics
  • Bacterial Outer Membrane Proteins / metabolism*
  • Cell Compartmentation
  • Cloning, Molecular
  • Cytoplasm / genetics
  • Cytoplasm / metabolism
  • Detergents
  • Escherichia coli / genetics
  • Glycosylation
  • Immunoblotting
  • Molecular Sequence Data
  • Protein Conformation
  • Pseudomonas / chemistry*
  • Pseudomonas / physiology
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / genetics
  • Recombinant Proteins / metabolism
  • Subcellular Fractions
  • Temperature

Substances

  • Bacterial Outer Membrane Proteins
  • Detergents
  • InaV protein, Pseudomonas syringae
  • Recombinant Proteins
  • ice nucleation protein

Associated data

  • GENBANK/AJ001086