This suggests that mRNA translation of the dsbI gene may be blocked due to the occlusion of the RBS, and that translation of the dba mRNA may make the RBS of the dsbI gene accessible and hence enable the translation of the dsbI gene as well. Verification of this hypothesis requires further analysis. This coupling mechanism may facilitate interaction between two proteins expressed from the same operon. Data obtained

in our study showed that in the absence of Dba, DsbI is intensively degraded in E. coli cells. Also in C. jejuni Δdba-dsbI::cat cells harboring a recombinant plasmid enabling expression of only DsbI, this protein migrates on SDS-PAGE slightly faster than DsbI produced by wild type cells. It was suggested by Cell Cycle inhibitor in silico analysis that the N-terminal domain of DsbI contains five transmembrane helixes CHIR98014 and its C-terminal domain learn more achieve a β-propeller structure and localize in the periplasm [18]. DsbI localization in the inner-membrane was documented by a cell fractionation experiment (data not shown). In silico prediction also localizes Dba in the IM. Although the specific mechanism of Dba and DsbI interplay is yet unknown, we hypothesize that Dba can act as a periplasmic or transmembrane chaperone, providing the proper

folding of the DsbI C-terminal domain, which might be a prerequisite for recruiting other proteins to form an active protein complex. Conclusions The present work documents that iron concentration is a significant factor influencing dsb gene transcription. Preliminary results of proteomic experiments aimed at identification of Campylobacter Dsb system targets suggest that Rucaparib molecular weight mutations in dsb genes influence the level of a dozen extracytoplasmic proteins (manuscript in preparation). One of them is the periplasmic LivJ protein, which contains four cysteine residues and is involved in the colonization process as shown by Hendrixon and DiRita [55]. Moreover proteomic analysis of iron-regulated C.

jejuni protein expression done by Holmes et al. showed that LivJ abundance is iron-dependent. Because livJ gene transcription is not iron nor Fur dependent, most likely the changes in the abundance of this protein are influenced by activity of the Dsb system [6]. Taken together, these results support the notion that iron concentration -through the influence on dsb gene expression – might control abundance of the extracytoplasmic proteins during different stages of infection. Our work further shows that the synthesis of the DsbI membrane oxidoreductase is controlled by a translational coupling mechanism. Among bacterial genomes sequenced so far, those of C. jejuni strains are extremely compact.