Identification and purification of a bacterial ice-nucleation protein.
AUTOR(ES)
Wolber, P K
RESUMO
The protein product of a gene (inaZ) responsible for ice nucleation by Pseudomonas syringae S203 has been identified and purified after overexpression in Escherichia coli. The amino acid composition and the N-terminal sequence of the purified, denatured protein corresponded well with that predicted from the sequence of the inaZ gene. The product of inaZ was also found to be the major component in preparations of ice-nucleating, proteinaceous particles, obtained after extraction with and gel filtration in a mixture of urea and the nondenaturing detergent octyl beta-D-thioglucopyranoside. The activity of these preparations in the absence of added lipid implies that the protein participates directly in the nucleation process.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=386694Documentos Relacionados
- Size of bacterial ice-nucleation sites measured in situ by radiation inactivation analysis
- Three separate classes of bacterial ice nucleation structures.
- Cloning and expression of bacterial ice nucleation genes in Escherichia coli.
- Identification and partial purification of the cardiac sodium-calcium exchange protein.
- Identification and purification of a protein that binds DNA cooperatively with the yeast SWI5 protein.
