Abstract
The critical collapse pressure of gas vesicles isolated from Anabaena flos-aquae decreased from 0.557 to 0.190 MPa when GvpC, the hydrophilic 22 kDa protein present on the outer surface of the gas vesicle, was removed by rising in 6 M urea. Recombinant GvpC was purified from inclusion bodies, produced in an E. coli strain containing an expression vector bearing the gene ecoding GvpC from A. flos-aquae, and then solubilised in 6 M urea. This recombinant GvpC became bound to gas vesicles that had been stripped of their native protein, when the urea was removed by dialysis; the amount which bound increased with the concentration of GvpC present. The critical pressure of these reconstituted gas vesicles increased to 0.533 MPa, 96% of the original value. These results indicate that the function of GvpC is to increase the strength of the structure.
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Abbreviations
- SBTI:
-
Soy bean trypsin inhibitor
- Gvp:
-
Gas vesicle protein
- SDS:
-
Sodium dodecyl sulphate
- PAGE:
-
Polyacrylamide gel electrophoresis
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Hayes, P.K., Buchholz, B. & Walsby, A.E. Gas vesicles are strengthened by the outer-surface protein, GvpC. Arch. Microbiol. 157, 229–234 (1992). https://doi.org/10.1007/BF00245155
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DOI: https://doi.org/10.1007/BF00245155