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Cloning and characterization of the Brucella ovis heat shock protein DnaK functionally expressed in Escherichia coli.


ABSTRACT: The Brucella ovis dnaK gene, homolog to the eukaryotic hsp70 genes, was cloned by using a Drosophila melanogaster probe. Comparison of B. ovis and Escherichia coli sequences revealed a similar organization for the dnaK and dnaJ genes and putative regulatory signals. In E. coli transfected with the cloned fragment, B. ovis hsp70 was expressed at 30 and 50 degrees C apparently under the control of its own promoter. The recombinant protein and a B. ovis native protein displaying the same molecular weight were both recognized by anti-E. coli DnaK serum. Native B. ovis protein was also recognized by sera of sheep either infected or vaccinated with an attenuated Brucella strain, suggesting that Brucella hsp70 could be up-regulated during host colonization. A thermosensitive E. coli dnaK mutant transfected with the cloned fragment recovered colony-forming ability at 42 degrees C, showing that the B. ovis DnaK protein could behave as a functional heat shock protein in E. coli.

SUBMITTER: Cellier MF 

PROVIDER: S-EPMC207542 | biostudies-other | 1992 Dec

REPOSITORIES: biostudies-other

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Cloning and characterization of the Brucella ovis heat shock protein DnaK functionally expressed in Escherichia coli.

Cellier M F MF   Teyssier J J   Nicolas M M   Liautard J P JP   Marti J J   Sri Widada J J  

Journal of bacteriology 19921201 24


The Brucella ovis dnaK gene, homolog to the eukaryotic hsp70 genes, was cloned by using a Drosophila melanogaster probe. Comparison of B. ovis and Escherichia coli sequences revealed a similar organization for the dnaK and dnaJ genes and putative regulatory signals. In E. coli transfected with the cloned fragment, B. ovis hsp70 was expressed at 30 and 50 degrees C apparently under the control of its own promoter. The recombinant protein and a B. ovis native protein displaying the same molecular  ...[more]

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