Subunit II of the <i>Paracoccus denitrificans</i> Cytochrome <i>c</i> Oxidase

Panskus, Gunnar; Steinrücke, Peter; Ludwig, Bernd

doi:10.1111/j.1749-6632.1988.tb35345.x

Cited by 4 publications

(1 citation statement)

References 14 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…In case of Paracoccus denitrificans this means that heterologous expression in E. coli is possible, although in most cases under the regime of an E. coli promoter. In fact the gene for subunit II of the cytochrome oxidase was cloned by an immune-screening procedure using the inducible lac-promoter for expression [52,107,108]. Likewise the fbcC-gene, being expressed under the control of the cat-promoter, has been cloned in pBR322 [31].…”

Section: Gc-content and Codon Usagementioning

confidence: 99%

Genetics of Paracoccus denitrificans

Steinrücke

Ludwig

1993

FEMS Microbiology Letters

View full text Add to dashboard Cite

Paracoccus has approx. 15 subunits [28]. The transcriptional organization of this NDH-l-cluster is presently unknown. NQ01 and NQ02 code for flavoproteins, NQ03 to NQ06 are genes for iron-sulfur proteins whereas NQ07 to NQ014 code for polypeptides of the hydrophobic protein fraction [28]. The gene order in this cluster is NQ07, NQ06, NQ05, NQ04, NO02, NQ01 NQ03, NQ08 NQ09, NQ010, NQ011, NQO12, NQ013, and NQ014.Upstream of NQ07 an open reading frame with homology to Escherichia coli uvrA is found. A reading frame with homology to E. coli biotin acetyl-CoA carboxylase ligase has been found downstream of the cluster [28].Sequences for two genes, NQ01 [29], encoding the NADH-binding subunit, and NQ02 [30], which codes for an iron-sulfur protein, have been published. Two URFs have been found; sequence similarities of URF2 to ctaG of the Paracoccus cta-operon suggest a possible role as an assembly protein, most probably in the attachment of iron [29,30,55]. Because of its simpler structure the Paracoccus complex is likely to play an important part in investigating inhibitory agents or the mode of complex formation during assembly. Mutant strains are presently not available.

show abstract

Section: Gc-content and Codon Usagementioning

confidence: 99%