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Biochem Biophys Res Commun. 1997 Oct 29;239(3):769-74.

A molecular aspect of symbiotic interactions between the weevil Sitophilus oryzae and its endosymbiotic bacteria: over-expression of a chaperonin.

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Laboratoire de Biologie Appliquée, INSA 406, UA-INRA 203, SDI-CNRS 5128, Villeurbanne, France.


Specific proteins of symbiosis were analyzed by the comparison of two-dimensional electrophoresis protein patterns of symbiotic and aposymbiotic strains of the weevil Sitophilus oryzae. One protein was shown to be exclusively expressed in the aposymbiotic strain and three proteins, including a chaperonin, were characterized in the symbiotic strain pattern. The groE-like operon, encoding the two chaperonins groES and GroEL-like proteins of the endocytobiotes, was sequenced. It was found to be very similar to the groE operon of Escherichia coli (82% identity). In vitro and ex vivo experiments of protein labelling demonstrated that almost 40% of the endocytobiote protein synthesis ex vivo is focused on the GroEL-like protein. Finally, we showed by northern blotting that heat shock at 38 degrees C results in groEL mRNA accumulation inside the endocytobiotes. This work supports the hypothesis that chaperonins could have an essential physiological function in the maintenance of the symbiotic association.

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