منابع مشابه
Protease secretion by Erwinia chrysanthemi. Proteases B and C are synthesized and secreted as zymogens without a signal peptide.
The gene encoding the secreted 53-kDa metalloprotease (protease B) and the 5' end of the gene encoding the secreted 55-kDa metalloprotease (protease C) of the Gram-negative bacterium Erwinia chrysanthemi have been sequenced. The predicted sequences of the two proteases do not have typical signal sequences at their NH2 termini. Both proteases are synthesized as inactive higher molecular weight p...
متن کاملLactose metabolism in Erwinia chrysanthemi.
Wild-type strains of the phytopathogenic enterobacterium Erwinia chrysanthemi are unable to use lactose as a carbon source for growth although they possess a beta-galactosidase activity. Lactose-fermenting derivatives from some wild types, however, can be obtained spontaneously at a frequency of about 5 X 10(-7). All Lac+ derivatives isolated had acquired a constitutive lactose transport system...
متن کاملSubset of hybrid eukaryotic proteins is exported by the type I secretion system of Erwinia chrysanthemi.
Erwinia chrysanthemi exports degradative enzymes by using a type I protein secretion system. The proteases secreted by this system lack an N-terminal signal peptide but contain a C-terminal secretion signal. To explore the substrate specificity of this system, we have expressed the E. chrysanthemi transporter system (prtDEF genes) in Escherichia coli and tested the ability of this ABC transport...
متن کاملLactose and melibiose metabolism in Erwinia chrysanthemi.
A Lac+ mutant of Erwinia chrysanthemi was isolated from the Lac- wild type on lactose agar. beta-Galactosidase was expressed independently of lactose transport in both the mutant and the wild type, and neither strain expressed thiogalactoside transacetylase. Lactose transport and alpha-galactosidase, constitutive in the Lac+ strain, were coordinately induced in the Lac- strain by melibiose and ...
متن کاملFunctional characterization of the Erwinia chrysanthemi OutS protein, an element of a type II secretion system.
Secretion of pectate lyases and a cellulase occurs in Erwinia chrysanthemi through a type II secretion machinery, the Out system. Proper insertion of the secretin OutD in the outer membrane requires the presence of OutS. OutS is an outer-membrane lipoprotein that interacts directly with OutD. Using ligand-blotting experiments, it has been shown that this interaction requires at least the 62 C-t...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1989
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)81905-6