Four colicin A double-cysteine mutants possessing a disulfide bond in their pore-forming domain were constructed to study the translocation and the pore formation of colicin A. The disulfide bonds connected α-helices 1 and 2, 2 and 10, 3 and 9, or 3 and 10 of the pore-forming domain. The disulfide bonds did not prevent the colicin A translocation through the Escherichia coli envelope. However, the mutated colicins were able to exert their in vivo channel activity only after reduction of their disulfide bonds. In vitro studies with brominated phospholipid vesicles and planar lipid bilayers revealed that the disulfide bond that connects the α-helices 2 and 10 prevented the colicin A membrane insertion, whereas the other double-cysteine mutant...
International audienceA bacterial signal sequence was fused to the colicin A pore-forming domain: th...
International audienceA bacterial signal sequence was fused to the colicin A pore-forming domain: th...
International audiencePore-forming colicins are soluble bacteriocins which form voltage-gated ion ch...
Four colicin A double-cysteine mutants possessing a disulfide bond in their pore-forming domain were...
Four colicin A double-cysteine mutants possessing a disulfide bond in their pore-forming domain were...
International audienceFour colicin A double-cysteine mutants possessing a disulfide bond in their po...
International audienceFour colicin A double-cysteine mutants possessing a disulfide bond in their po...
International audienceFour colicin A double-cysteine mutants possessing a disulfide bond in their po...
Four colicin A double-cysteine mutants possessing a disulfide bond in their pore-forming domain were...
Four colicin A double-cysteine mutants possessing a disulfide bond in their pore-forming domain were...
International audienceFour disulfide bonds were engineered into the pore-forming domain of colicin A...
International audienceThree double cysteine mutants, each possessing a disulfide bond in its pore-fo...
International audienceThree double cysteine mutants, each possessing a disulfide bond in its pore-fo...
International audienceThree double cysteine mutants, each possessing a disulfide bond in its pore-fo...
International audienceThree double cysteine mutants, each possessing a disulfide bond in its pore-fo...
International audienceA bacterial signal sequence was fused to the colicin A pore-forming domain: th...
International audienceA bacterial signal sequence was fused to the colicin A pore-forming domain: th...
International audiencePore-forming colicins are soluble bacteriocins which form voltage-gated ion ch...
Four colicin A double-cysteine mutants possessing a disulfide bond in their pore-forming domain were...
Four colicin A double-cysteine mutants possessing a disulfide bond in their pore-forming domain were...
International audienceFour colicin A double-cysteine mutants possessing a disulfide bond in their po...
International audienceFour colicin A double-cysteine mutants possessing a disulfide bond in their po...
International audienceFour colicin A double-cysteine mutants possessing a disulfide bond in their po...
Four colicin A double-cysteine mutants possessing a disulfide bond in their pore-forming domain were...
Four colicin A double-cysteine mutants possessing a disulfide bond in their pore-forming domain were...
International audienceFour disulfide bonds were engineered into the pore-forming domain of colicin A...
International audienceThree double cysteine mutants, each possessing a disulfide bond in its pore-fo...
International audienceThree double cysteine mutants, each possessing a disulfide bond in its pore-fo...
International audienceThree double cysteine mutants, each possessing a disulfide bond in its pore-fo...
International audienceThree double cysteine mutants, each possessing a disulfide bond in its pore-fo...
International audienceA bacterial signal sequence was fused to the colicin A pore-forming domain: th...
International audienceA bacterial signal sequence was fused to the colicin A pore-forming domain: th...
International audiencePore-forming colicins are soluble bacteriocins which form voltage-gated ion ch...