Secretory S complex of Bacillus subtilis: sequence analysis and identity to pyruvate dehydrogenase

Hemilä, Harri; Palva, Airi; Paulín, Lars; Arvidson, Staffan; Palva, Ilkka

doi:10.1128/jb.172.9.5052-5063.1990

Cited by 97 publications

(68 citation statements)

References 72 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…7B). The amino acid sequencing revealed that the 65 kDa protein was pyruvate dehydrogenase C (PdhC; data not shown), which has been known to be a component of the membrane-bound S complex (Hemila et al, 1990). By electron microscopy, among the HBB complexes we observed many small particles of c. 45 nm in diameter, as described previously (Caulfield et al, 1985).…”

Section: Pdhcsupporting

confidence: 71%

Purification and characterization of the flagellar hook–basal body complex of Bacillus subtilis

Kubori

Okumura

Kobayashi

et al. 1997

Molecular Microbiology

View full text Add to dashboard Cite

SummaryThe flagellar hook-basal body (HBB) complex of the Gram-positive bacterium Bacillus subtilis was purified and analysed by electron microscopy, gel electrophoresis, and amino acid sequencing of the major component proteins. The purified HBB complex consisted of the inner (M and S) rings, a rod and a hook. There were no outer (P and L) rings that are found in Gram-negative bacteria. The hook was 15 nm in thickness and 70 nm in length, which is thinner and longer than the hook of Salmonella typhimurium. The hook protein had an apparent molecular mass of 29 kDa, and its N-terminal sequence was identical to that of B. subtilis FlgG

show abstract

Section: Pdhcsupporting

confidence: 71%

Purification and characterization of the flagellar hook–basal body complex of Bacillus subtilis

Kubori

Okumura

Kobayashi

et al. 1997

Molecular Microbiology

View full text Add to dashboard Cite

show abstract

“…Many species seem to have a single lipoamide dehydrogenase which functions as the E3 component of pyruvate, ␣-ketoglutarate, and BCDHs. In humans and B. subtilis, the E3 component of the PDH complex is shared by the three ␣-keto acid dehydrogenases (27,48). The data suggest that the S. avermitilis genes reported here may have an organization similar to that of the B. subtilis cluster of genes encoding the BCDH responsible for branched-chain fatty acid synthesis, which consists of E1␣, E1␤, and E2 genes in the same orientation (64).…”

Section: Vol 177 1995mentioning

confidence: 58%

“…E3 (10,11,26,27,59). Recently, the genes for the branchedchain fatty acid-specific BCDH from B. subtilis were cloned and sequenced (64).…”

mentioning

confidence: 99%

“…In these systems, it was found that the genes encoding the BCDH complex were clustered in an operon. The genes encoding the BCDH complex of P. putida (bkd genes) and the PDH/BCDH dual complex of B. subtilis and Bacillus stearothermophilus are clustered in the sequence E1␣, E1␤, E2, and E3 (10,11,26,27,59). Recently, the genes for the branchedchain fatty acid-specific BCDH from B. subtilis were cloned and sequenced (64).…”

mentioning

confidence: 99%

See 1 more Smart Citation

Cloning and sequencing of a cluster of genes encoding branched-chain alpha-keto acid dehydrogenase from Streptomyces avermitilis and the production of a functional E1 [alpha beta] component in Escherichia coli

et al. 1995

View full text Add to dashboard Cite

A cluster of genes encoding the E1␣, E1␤, and E2 subunits of branched-chain ␣-keto acid dehydrogenase (BCDH) of Streptomyces avermitilis has been cloned and sequenced. Open reading frame 1 (ORF1) (E1␣), 1,146 nucleotides long, would encode a polypeptide of 40,969 Da (381 amino acids). ORF2 (E1␤), 1,005 nucleotides long, would encode a polypeptide of 35,577 Da (334 amino acids). The intergenic distance between ORF1 and ORF2 is 73 bp. The putative ATG start codon of the incomplete ORF3 (E2) overlaps the stop codon of ORF2. Computer-aided searches showed that the deduced products of ORF1 and ORF2 resembled the corresponding E1 subunit (␣ or ␤) of several prokaryotic and eukaryotic BCDH complexes. When these ORFs were overexpressed in Escherichia coli, proteins of about 41 and 34 kDa, which are the approximate masses of the predicted S. avermitilis ORF1 and ORF2 products, respectively, were detected. In addition, specific E1[␣␤] BCDH activity was detected in E. coli cells carrying the S. avermitilis ORF1 (E1␣) and ORF2 (E1␤) coexpressed under the control of the T7 promoter.The branched-chain ␣-keto acid dehydrogenase (BCDH) complex catalyzes the oxidative decarboxylations of ␣-ketoisovalerate, ␣-keto-␤-methylvalerate, and ␣-ketoisocaproate (the deamination products of the branched-chain amino acids valine, isoleucine, and leucine, respectively), releasing CO 2 and generating the corresponding acyl-coenzyme A and NADH (36). The enzyme has been characterized from several sources, including Pseudomonas putida (55), Pseudomonas aeruginosa (39), Bacillus subtilis (37), rabbit liver (46), and bovine and rat kidneys (43, 49). The purified complexes from P. putida, P. aeruginosa, B. subtilis, and several mammals are all composed of four polypeptides, E1␣, E1␤, E2, and E3, with three different catalytic activities: a BCDH and decarboxylase (E1[␣␤]), a dihydrolipoamide acyltransferase (E2), and a dihydrolipoamide dehydrogenase (E3). The E1[␣␤] component requires thiamine pyrophosphate (TPP) as a cofactor and possesses a structural binding motif that resembles those of many of the TPP-binding enzymes (25). The BCDH complex has structural and enzymatic properties similar to those of pyruvate dehydrogenase (PDH) and ␣-ketoglutarate dehydrogenase complexes (48, 69). Interestingly, a dual-purpose ␣-keto acid dehydrogenase complex which has both pyruvate and BCDH activities has been isolated from B. subtilis (37). In addition, an exclusive BCDH which is essential for branchedchain fatty acid synthesis has been isolated from B. subtilis (44).Cloning of prokaryotic BCDH genes has been reported for Pseudomonas and Bacillus species but not for Streptomyces species. In these systems, it was found that the genes encoding the BCDH complex were clustered in an operon. The genes encoding the BCDH complex of P. putida (bkd genes) and the PDH/BCDH dual complex of B. subtilis and Bacillus stearothermophilus are clustered in the sequence E1␣, E1␤, E2, and E3 (10,11,26,27,59). Recently, the genes for the branchedchain fatty acid-specific BCDH fr...

show abstract

“…9) shows clearly that the conserved residues (reverse shading) are found in the M. capricolum sequence. Boxes shaded in grey cor- laidlawii (odpb-achla) (Wallbrandt et al, 1992); B. subtilis (odpb-bacsu) (Hemila et al, 1990) and (odbb-bacsu) (Wang et al, 1993); E. stearothermophilus (odpb-bacst) (Borges et al, 1990), human (odbb-human) (Nobukuni et al, 1990a) and (odpb-human) (Ho & Patel, 1990); bovine (odbb-bovin) (Nobukuni et al, 1990b); rat (odbb-rat) (Zhao et al, 1992); P. putida (odbb-psepu) (Burns et al, 1988); A . suum (odpb-ascu) (Wheelock et al, 1991); yeast (odpb-yeast) (Miran et al, 1993); A .…”

Section: O O a I L C " T P A T T A O A T T M T~t A T~~a~m C -~A~~g K~mentioning

confidence: 99%

Sequence and organization of genes encoding enzymes involved in pyruvate metabolism in mycoplasma capricolum

Zhu

Peterkofsky

1996

Protein Science

View full text Add to dashboard Cite

The region of the genome of Mycoplasma capricolum upstream of the portion encompassing the genes for Enzymes I and IIAg" of the phosphoeno1pyruvate:sugar phosphotransferase system (PTS) was cloned and sequenced. Examination of the sequence revealed open reading frames corresponding to numerous genes involved with the oxidation of pyruvate. The deduced gene organization is naox (encoding NADH oxidase)-lplA (encoding lipoate-protein ligase)-odpA (encoding pyruvate dehydrogenase EIa)-odpB (encoding pyruvate dehydrogenase EIP)-odp2 (encoding pyruvate dehydrogenase EI1)-dldH (encoding dihydrolipoamide dehydrogenase)-pta (encoding phosphotransacety1ase)-ack (encoding acetate kinase)-orfA (an unknown open reading frame)-kdtB-ptsl-crr. Analysis of the DNA sequence suggests that the naox and IpIA genes are part of a single operon, odpA and odpB constitute an additional operon, odp2 and dldH a third operon, andpta and ack an additional transcription unit. Phylogenetic analyses of the protein products of the odpA and odpB genes indicate that they are most similar to the corresponding proteins from Mycoplasma genitalium, Acholeplasma laidlawii, and Gram-positive organisms. The product of the odp2 gene contains a single lipoyl domain, as is the case with the corresponding proteins from M. genitalium and numerous other organisms. An evolutionary tree places the M. capricolum odp2 gene product in close relationship to the corresponding proteins from A. laidlawii and M. genitalium. The dldH gene encodes an unusual form of dihydrolipoamide dehydrogenase that contains an aminoterminal extension corresponding to a lipoyl domain, a property shared by the corresponding proteins from Alcaligenes eutrophus and Clostridium magnum. Aside from that feature, the protein is related phylogenetically to the corresponding proteins from A. laidlawii and M. genitalium. The phosphotransacetylase from M. capricolum is related most closely to the corresponding protein from M. genitalium and is distinguished easily from the enzymes from Escherichia coli and Haemophilus influenzae by the absence of the characteristic amino-terminal extension. The acetate kinase from M. capricolum is related evolutionarily to the homologous enzyme from M. genitalium. Map position comparisons of genes encoding proteins involved with pyruvate metabolism show that, whereas all the genes are clustered in M. capricolum, they are scattered in M. genitalium.

show abstract

Secretory S complex of Bacillus subtilis: sequence analysis and identity to pyruvate dehydrogenase

Cited by 97 publications

References 72 publications

Purification and characterization of the flagellar hook–basal body complex of Bacillus subtilis

Purification and characterization of the flagellar hook–basal body complex of Bacillus subtilis

Cloning and sequencing of a cluster of genes encoding branched-chain alpha-keto acid dehydrogenase from Streptomyces avermitilis and the production of a functional E1 [alpha beta] component in Escherichia coli

Sequence and organization of genes encoding enzymes involved in pyruvate metabolism in mycoplasma capricolum

Contact Info

Product

Resources

About