Organization and nucleotide sequences of the genes encoding the biotin carboxyl carrier protein and biotin carboxylase protein of Pseudomonas aeruginosa acetyl coenzyme A carboxylase

Best, E A; Knauf, Vic

doi:10.1128/jb.175.21.6881-6889.1993

Cited by 38 publications

(33 citation statements)

References 33 publications

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“…A putative ribosome-binding site (-ACGAG-) was located 6 bp upstream of the dipZ start codon. A second ORF of 441 nt, sequenced but not reported by Best & Knauf (1993), was identified in the dipZ-accB intergenic region. The predicted protein product of this ORF exhibited striking homology to the catabolic dehydroquinase AroQ of Actinobacillus pleuropneumoniae (Lalonde et al, 1994) and it was named accordingly.…”

Section: Resultsmentioning

confidence: 99%

“…This region was located from 610 to 860 bp upstream of the P . aeruginosa P A 0 1 accB gene (Best & Knauf, 1993) (Fig. 1).…”

Section: Resultsmentioning

confidence: 99%

“…The following strains and plasmids were used in this study: P . pBR322 (Sutcliffe, 1979) ; pCGN3941 (Best & Knauf, 1993) ; pLitmus38 (New England Biolabs) ; pRVS1 (van Spanning et al, 1991) ; pUC18 (Yanisch-Perron et al, 1985). P .…”

Section: Methodsmentioning

confidence: 99%

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Disruption of the Pseudomonas aeruginosa dipZ gene, encoding a putative protein-disulfide reductase, leads to partial pleiotropic deficiency in c-type cytochrome biogenesis

1997

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The Pseudomonas eenrginou) dip2 gene has been cloned and sequenced. Whereas disruption of Escherichie COIi dip2 (dolbD), the hydrophilic C-terminal domain of which has been deduced to be periplasmic and to function as a protein-disulfide reductase, leads to the absence of c-type cytochromes, disruption of P. aenrginou) dip2 attenuated, but did not abolish, holo-c-type cytochrome biosynthesis. Comparison of the P. aenrginosa DipZ sequence with three other DipZ sequences indicated that there are not only two conserved cysteine residues in the C-terminal hydrophilie domain, but also two more in the central highly hydrophobic domain. The latter would be located toward the centre of two of the eight membrane-spanning oc-helices predicted t o compose the hydrophobic central domain of DipZ. Both these cysteine residues, plus other transmembrane helix residues, notably prolines and glycines, are also conserved in a t ( w p of membrane proteins, related t o Bacillus subtilis CcdA, which lack the N-and C-terminal hydrophilic domains of the DipZ proteins. It is proposed that Dip2 of P. eenrginosa and other organisms transfers reducing power from the cytoplasm t o the periplasm through reduction and reoxidation of an intramembrane disulf ide bond, or other mechanism involving these cysteine residues, and that this function can also be performed by B. subtoltr CcdA and other CcdA-like proteins. The failure of dip2 disruption to abolish etype cytochrome synthesis in P. eenrginosa suggests that, in contrast to the situation in E. d i , the absence of DipZ can be compensated for by one or more other proteins, for example a CcdA-like protein acting in tandem with one or more thioredoxin-like proteins.

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Section: Resultsmentioning

confidence: 99%

“…This region was located from 610 to 860 bp upstream of the P . aeruginosa P A 0 1 accB gene (Best & Knauf, 1993) (Fig. 1).…”

Section: Resultsmentioning

confidence: 99%

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Disruption of the Pseudomonas aeruginosa dipZ gene, encoding a putative protein-disulfide reductase, leads to partial pleiotropic deficiency in c-type cytochrome biogenesis

1997

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“…The molecular masses on SDS-PAGE of biotin carboxyl carrier proteins of acetyl-CoA carboxylases from E. coli, Anabaena sp. strain PCC 7120, and Pseudomonas aeruginosa are 22 to 25 kDa (3,11,26). Since the 31-kDa protein was similar to these proteins in size, M. xanthus may have another acetyl-CoA carboxylase, like the enzyme from E. coli.…”

Section: Discussionmentioning

confidence: 99%

Molecular Cloning and Characterization of Two Genes for the Biotin Carboxylase and Carboxyltransferase Subunits of Acetyl Coenzyme A Carboxylase in Myxococcus xanthus

et al. 2000

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We have cloned a DNA fragment from a genomic library of Myxococcus xanthus using an oligonucleotide probe representing conserved regions of biotin carboxylase subunits of acetyl coenzyme A (acetyl-CoA) carboxylases. The fragment contained two open reading frames (ORF1 and ORF2), designated the accB and accA genes, capable of encoding a 538-amino-acid protein of 58.1 kDa and a 573-amino-acid protein of 61.5 kDa, respectively. The protein (AccA) encoded by the accA gene was strikingly similar to biotin carboxylase subunits of acetyl-CoA and propionyl-CoA carboxylases and of pyruvate carboxylase. The putative motifs for ATP binding, CO 2 fixation, and biotin binding were found in AccA. The accB gene was located upstream of the accA gene, and they formed a two-gene operon. The protein (AccB) encoded by the accB gene showed high degrees of sequence similarity with carboxyltransferase subunits of acetyl-CoA and propionyl-CoA carboxylases and of methylmalonyl-CoA decarboxylase. Carboxybiotin-binding and acyl-CoA-binding domains, which are conserved in several carboxyltransferase subunits of acyl-CoA carboxylases, were found in AccB. An accA disruption mutant showed a reduced growth rate and reduced acetyl-CoA carboxylase activity compared with the wild-type strain. Western blot analysis indicated that the product of the accA gene was a biotinylated protein that was expressed during the exponential growth phase. Based on these results, we propose that this M. xanthus acetyl-CoA carboxylase consists of two subunits, which are encoded by the accB and accA genes, and occupies a position between prokaryotic and eukaryotic acetyl-CoA carboxylases in terms of evolution.

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“…coli ACC consists of a dimer of 49-kDa BC monomers, a dimer of 17-kDa BCCP monomers, and a CT tetramer containing two 33-kDa and two 35-kDa subunits. The primary structures of all of the E. coli ACC subunits (4)(5)(6)(7)(8), as well as the structures of the BC and BCCP of Anabaena 7120 (9), Synechoccocus 7942 (L. Phung and R.H., unpublished work), and P. aeruginosa (10), are known, based on the gene sequences. The genes encoding the subunits of E. coli ACC are called accA (CT a subunit), accB (BCCP), accC (BC), and accD (CT (3 subunit).…”

mentioning

confidence: 99%

Wheat acetyl-coenzyme A carboxylase: cDNA and protein structure.

Górnicki

Podkowiński

Scappino

et al. 1994

Proc. Natl. Acad. Sci. U.S.A.

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Organization and nucleotide sequences of the genes encoding the biotin carboxyl carrier protein and biotin carboxylase protein of Pseudomonas aeruginosa acetyl coenzyme A carboxylase

Cited by 38 publications

References 33 publications

Disruption of the Pseudomonas aeruginosa dipZ gene, encoding a putative protein-disulfide reductase, leads to partial pleiotropic deficiency in c-type cytochrome biogenesis

Disruption of the Pseudomonas aeruginosa dipZ gene, encoding a putative protein-disulfide reductase, leads to partial pleiotropic deficiency in c-type cytochrome biogenesis

Molecular Cloning and Characterization of Two Genes for the Biotin Carboxylase and Carboxyltransferase Subunits of Acetyl Coenzyme A Carboxylase in Myxococcus xanthus

Wheat acetyl-coenzyme A carboxylase: cDNA and protein structure.

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