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 Campylobacter 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.

journal_name

Curr Microbiol

journal_title

Current microbiology

authors

Aliouane S,Pagès JM,Bolla JM

doi

10.1007/s00284-015-0980-x

subject

Has Abstract

pub_date

2016-05-01 00:00:00

pages

511-7

issue

5

eissn

0343-8651

issn

1432-0991

pii

10.1007/s00284-015-0980-x

journal_volume

72

pub_type

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