Molecular organisation of the ice nucleation protein InaV from Pseudomonas syringae

• Published in: FEBS letters Vol. 414; no. 3; pp. 590 - 594
• Main Authors: Schmid, Daniel, Pridmore, David, Capitani, Guido, Battistutta, Roberto, Neeser, Jean-Richard, Jann, Alfred
• Format: Journal Article
• Language: English
• Published: England Elsevier B.V 15.09.1997
• Subjects: Bacterial ice nucleation; 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; inaV sequence; Molecular Sequence Data; Protein aggregation; Protein Conformation; Pseudomonas - chemistry; Pseudomonas - physiology; Pseudomonas syringae; Recombinant Proteins - chemistry; Recombinant Proteins - genetics; Recombinant Proteins - metabolism; Subcellular Fractions; Temperature; β-strand; Bacterial ice nucleation; Protein aggregation; inaV sequence; β-strand; Pseudomonas syringae
• ISSN: 0014-5793; 1873-3468
• DOI: 10.1016/S0014-5793(97)01079-X

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 β-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.