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Cloning, Expression, Purification, Regulation, and Subcellular Localization of a Mini-protein from Campylobacter jejuni

Abstract : The Cj1169c-encoded putative protein of Campylobacter was expressed and purified from E. coli after sequence optimization. The purified protein allowed the production of a specific rabbit antiserum that was used to study the protein expression in vitro and its subcellular localization in the bacterial cell and putative interactions with other proteins. This protein is produced in Campy- lobacter and it clearly localizes into the periplasmic space. The level of protein production depends on factors, including pH, temperature, osmolarity, and growth phase suggesting a role in the Campylobacter environmental adaptation. The cysteine residues present in the sequence are probably involved in disulfide bridges, which may promote covalent interactions with other proteins of the Campylobacter envelope.
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Contributor : Jean-Marie Pages <>
Submitted on : Thursday, February 16, 2017 - 3:53:48 PM
Last modification on : Tuesday, January 30, 2018 - 1:30:28 AM
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Soumeya Aliouane, Jean-Marie Pages, Jean-Michel Bolla. Cloning, Expression, Purification, Regulation, and Subcellular Localization of a Mini-protein from Campylobacter jejuni. Current Microbiology, Springer Verlag, 2016, ⟨10.1007/s00284-015-0980-x⟩. ⟨hal-01463172⟩

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