Molecular organisation of the ice nucleation protein InaV from Pseudomonas syringae.
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.
Schmid
D
D
Nestlé Research Center, Nestec Ltd., Lausanne, Switzerland. daniel.schmid@chlsnr.nestrd.ch
Pridmore
D
D
Capitani
G
G
Battistutta
R
R
Neeser
J R
JR
Jann
A
A
D001425:Bacterial Outer Membrane Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D002451:Cell Compartmentation; D003001:Cloning, Molecular; D003593:Cytoplasm / Q000235:genetics / Q000378:metabolism; D003902:Detergents; D004926:Escherichia coli / Q000235:genetics; D006031:Glycosylation; D015151:Immunoblotting; D008969:Molecular Sequence Data; D011487:Protein Conformation; D011549:Pseudomonas / Q000737:chemistry* / Q000502:physiology; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D013347:Subcellular Fractions; D013696:Temperature
D001425:Bacterial Outer Membrane Proteins; D003902:Detergents; C108515:InaV protein, Pseudomonas syringae; D011994:Recombinant Proteins; C063113:ice nucleation protein