Open AccessThe sequence of the major gas vesicle protein, GvpA, influences the width and strength of halobacterial gas vesicles
Author(s) -
Beard Steven J.,
Hayes Paul K.,
Pfeifer Felicitas,
Walsby Anthony E.
Publication year - 2002
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.2002.tb11299.x
Subject(s) - haloferax volcanii , vesicle , halobacterium salinarum , halophile , archaea , biochemistry , biology , chemistry , bacteria , gene , genetics , membrane
Transformation experiments with Haloferax volcanii show that the amino acid sequence of the gas vesicle protein GvpA influences the morphology and strength of gas vesicles produced by halophilic archaea. A modified expression vector containing p‐ gvpA was used to complement a Vac − strain of Hfx. volcanii that harboured the entire p‐vac region (from Halobacterium salinarum PHH1) except for p‐ gvpA . Replacement of p‐ gvpA with mc‐ gvpA (from Haloferax mediterranei ) led to the synthesis of gas vesicles that were narrower and stronger. Other gene replacements (using c‐ gvpA from Hbt. salinarum or mutated p‐ gvpA sequences) led to a significant but smaller increase in gas vesicle strength, and less marked effects on gas vesicle morphology.