Characterization of cDNAs encoding human pyruvate dehydrogenase alpha subunit.

Ho, Lap; Wexler, Isaiah D.; Liu, Te-Chung; Thekkumkara, Thomas J.; Patel, Mulchand S.

doi:10.1073/pnas.86.14.5330

Cited by 39 publications

(18 citation statements)

References 24 publications

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“…Components of enzymes involved in oxidative decarboxylation (dihydrolipoamide succinyl transferase, 31 the puruvate dehydrogenase E-1 subunit 32 and the electron transport chain [NADH dehydrogenase 1␤ subcomplex 10 33 ]) were up-regulated by androgen. VDAC-2, 34 a member of the group of small pore-forming proteins of the outer mitochondrial membrane, which may regulate the transport of small metabolites necessary for oxidative phosphorylation, was also up-regulated by androgen.…”

Section: Biochemical and Biologic Properties Of The Args Identified Bmentioning

confidence: 99%

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Quantitative expression profile of androgen-regulated genes in prostate cancer cells and identification of prostate-specific genes

Labiche

et al. 2001

Int. J. Cancer

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Section: Biochemical and Biologic Properties Of The Args Identified Bmentioning

confidence: 99%

“…PolyA ϩ RNA prepared from these cells was fractionated (2 g/lane) by a run through 1% formaldehyde-agarose gel and transferred to a nylon membrane. cDNA probes of five representative ARGs (PSA, 16 32 PdCTP, and Northern hybridization was performed as described before. 18 …”

Section: Northern Blot Analysis Of Argsmentioning

confidence: 99%

Quantitative expression profile of androgen-regulated genes in prostate cancer cells and identification of prostate-specific genes

Labiche

et al. 2001

Int. J. Cancer

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“…In additi on, the stretch of amino acids encoded by this exon and the contiguous phosphorylation site I is highly conserved both in length and in am ino acid homology when a comparison is made between the a -subunits from multiple species, both euka ryotic and prokaryotic, of the a -keto acid deh ydrogenase complexes (Fig. 6A) (10,26,(29)(30)(31)(32)(33)(34)(35)(36). Th e structure ofthis region is also intere sting.…”

Section: Variable Expression Of Pdc Defici Encymentioning

confidence: 99%

“…Th e seq uence and location of the prim ers used for reverse tran scription and DNA ampl ification are shown in Figure 1. Reverse transcription of 1 to 4 J. Lg of total RNA was performed as previously described (10,24). Th e products of this reaction were amplified by PCR using Taq polymerase (Perkin Elmer Cetus , Norwalk , CT) and a DNA therm al cycler (Perkin Elmer Cetus).…”

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confidence: 99%

A Mutation in the E1α Subunit of Pyruvate Dehydrogenase Associated with Variable Expression of Pyruvate Dehydrogenase Complex Deficiency

et al. 1992

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ABSTRACT. Defects in pyruvate dehydrogenase, the first catalytic component of the pyruvate dehydrogenase complex, are the most common cause of pyruvate dehydrogenase complex deficiency. A family with variable pyruvate dehydrogenase complex deficiency had been described in which cultured skin fibroblast s of affected family members had normal pyruvate dehydrogenase complex activity, but different tissues and blood lymphocytes had significantly diminished activities. Enzymatic activity and immunoblot studies indicated that pyruvate dehydrogenase was affected. Further evidence is presented here showing that the defect affecting pyruvate dehydrogenase complex activity is posttranscriptional. Sequencing of the coding region of the a -subunit of pyruvate dehydrogenase revealed a point mutation in the codon for amino acid 234 resulting in a substitution of glycine for arginine. Stud y of other members of the family suggested that this mutation is inherited in a sex-linked mode. The point mutation is located in a highly conserved region of the pyruvate dehydrogenase a-subunit gene that contains both hydrophobic and positively charged amino acid residues. Variable expression of pyruvate dehydrogenase complex deficiency in this case may be due to instability of the pyruvate dehydrogenase heterotetramer in specific tissues because of a disruption in subunit-subunit interaction. (Pediatr Res 32: 169-174,1992) Abbreviations Ell pyruvate dehydrogenase E1a , a -subunit of E. E 1,8 , ,8-subunit of E 1 E3, dihydrolipoamide dehydrogenase PDC, pyruvate dehydrogenase complex PCR, polymerase chain reaction Th e PDC is a nuclear-encoded mitochondrial enzyme complex t hat catalyzes the conversion of pyruvate to acetyl-CoA. PDC consists of thre e catalytic components: E 1 (pyruvate:lipoam ide 2-oxidoreductase, EC 1.2.4.1.), dihydrolipoamide acetyltransferase, and E 3 as well as a prot ein X that forms part of the comp lex. The E 1 com ponent consists of two subunits encoded by different genes, a and (3, which com bine as a heterotetramer. Regulation of the complex is via phosphorylation by Ei-kinase and dephosphorylation by phospho E j-phosphatase of th ree specific serine residues on Ela (1,2).PDC deficiency, an inborn error of pyruvate metabolism, is manifested by elevated serum pyruvat e and lactate. Individuals with PDC deficiency have varying levels of neur ologic dysfunction ranging from mild ataxia to neuroanatom icallesions incompatible with life (3, 4). Most PDC mutations affect the E1 component of PDC (5, 6). Recently, identification of mut ations affecting Ela has been facilitated by the cloning and charac terization of cDNA (7-10) and genomic DNA for Eta (1 1, 12). By in situ hybridization, the Ela gene has been localized to the X chromosome (13). Mutations involving deletions or single base changes have been found on the a -subunit (14-17).Previously, we described a family with PDC deficiency in which variable PDC enzymatic activity was observed in different tissues (18). The proband was found to have minimal PDC activi...

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“…FASTA analysis showed the protein product to be the a-subunit of pyruvate dehydrogenase Enzyme I. Figure 5 shows (Ho et al ., 1989), and (odpt-human) (Dah1 et al, 1987); pig (odpa-pig) (Sermon et al, 1990); mouse (odpa-mouse) (Fitzgerald et al, 1992) and (odpt-mouse) (Fitzgerald et al, 1992); rat (odba-rat) (Zhang et al, 1987), (odpt-rat) (Cullingford et a]., 1993), and (odpa-rat) (Cullingford et al, 1994); Ascarus suum (odpt-ascu) (Johnson et al, 1992) and (odpa-ascu) (Johnson et al, 1992); C. magnum (acoa-cloma) (Kruger et a]., 1994); A . eutrophus (acoaalceu) (Priefert et al, 1991); Pelobucter carbinolicus (acoa-pelca) ; K. pneumoniae (acoa-klepn) (Deng et al, 1994); bovine (odba-bovin) ; Pseudomonasputidu (odba-psepu) (Burns et al, 1988).…”

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~unclassified

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

Zhu

Peterkofsky

1996

Protein Science

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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.

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Characterization of cDNAs encoding human pyruvate dehydrogenase alpha subunit.

Abstract: A cDNA clone (1423 base pairs) comprising the entire coding region of the precursor form of the a subunit of pyruvate dehydrogenase (Ela)

Cited by 39 publications

References 24 publications

Quantitative expression profile of androgen-regulated genes in prostate cancer cells and identification of prostate-specific genes

Quantitative expression profile of androgen-regulated genes in prostate cancer cells and identification of prostate-specific genes

A Mutation in the E1α Subunit of Pyruvate Dehydrogenase Associated with Variable Expression of Pyruvate Dehydrogenase Complex Deficiency

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

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