Molecular organisation of the ice nucleation protein InaV from Pseudomonas syringae

FEBS Letters

Neeser, Jean-Richard¹  Pridmore, David¹  Battistutta, Roberto²  Capitani, Guido³  Schmid, Daniel¹  Jann, Alfred¹ 

[1]Nestlé Research Center, Nestec Ltd., Vers-chez-les-Blanc, P.O. Box 44, 1000 Lausanne 26, Switzerland

[2]Dipartimento di Chimica Organica, Università degli Studi di Padova, via Marzolo 1, 35131 Padua, Italy

[3]Abteilung Strukturbiologie, Biozentrum der Universität Basel, Klingerbergstrasse 70, 4056 Basel, Switzerland

关键词: Bacterial ice nucleation;    inaV sequence;    Protein aggregation;    β-strand;    Pseudomonas syringae;   

DOI  :  10.1016/S0014-5793(97)01079-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown