Disease relevance of dipZ

• In contrast, dsbC and dsbD mutants showed no hypersensitivity [1].
• Escherichia coli JCB606 carries a mutation in the dipZ gene, known to code for a disulphide isomerase-like protein, with the consequence that holo forms of neither exogenous nor endogenous c-type cytochromes are synthesised [2].
• The Pseudomonas aeruginosa dipZ gene has been cloned and sequenced [3].

High impact information on dipZ

• A search for extragenic mutations able to compensate for the lack of dsbA function in vivo led us to the identification of a new gene, designated dsbD [4].
• Expressing this subdomain in the periplasmic space helped restore the phenotypic defects associated with a dsbD null mutation [4].
• We further show that in dsbD mutant bacteria the dithiol active sites of DsbA and DsbC proteins are mostly oxidized, as compared with wild-type bacteria [4].
• In addition, unlike the rest of the dsb genes, dsbD is essential for bacterial growth at temperatures above 42 degrees C. Cloning of the wild-type gene and sequencing and overexpression of the protein show that dsbD is part of an operon and encodes an inner membrane protein [4].
• Mutations in the dipZ and trxA genes have similar phenotypes [5].

Biological context of dipZ

• In contrast, only the dsbB and dipZ (dsbD) strains were defective in periplasmic nitrate reductase activity, suggesting that DsbB might fulfil an additional role in anaerobic electron transport [6].
• In contrast, the R. capsulatus ccdA was homologous to the cyt c biogenesis gene ccdA, found in the gram-positive bacterium Bacillus subtilis, and to the central region of dipZ, encoding a protein disulphide reductase required for cyt c biogenesis in Escherichia coli [7].
• An internal deletion of a portion of htrI encoding the putative methylation and signaling domains of HtrI (253 residues) prevents the restoration of phototaxis, providing further evidence for the role of HtrI as a transducer for SR-I [8].

Associations of dipZ with chemical compounds

• Coexpression of the methyl-accepting protein gene (designated htrI) and sopI restores sensory rhodopsin I phototaxis to a mutant (Pho81) that contains a deletion in the htrI/sopI region [9].

References