Premium
Molecular organisation of the ice nucleation protein InaV from Pseudomonas syringae
Author(s) -
Schmid Daniel,
Pridmore David,
Capitani Guido,
Battistutta Roberto,
Neeser Jean-Richard,
Jann Alfred
Publication year - 1997
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(97)01079-x
Subject(s) - pseudomonas syringae , ice nucleus , microbiology and biotechnology , pseudomonadaceae , pseudomonas , pseudomonadales , nucleation , chemistry , biology , bacteria , genetics , pathogen , organic chemistry
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.