The pyruvate dehydrogenase complex of Mycoplasma hyopneumoniae contains a novel lipoyl domain arrangement

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Show simple item record Matic, Jake en_US Wilton, Judy en_US Towers, Rebecca en_US Scarmann, Anthony en_US Minion, F. Chris en_US Walker, Mark en_US Djordjevic, Steven en_US
dc.contributor.editor en_US 2010-05-28T09:44:41Z 2010-05-28T09:44:41Z 2003 en_US
dc.identifier 2008007041 en_US
dc.identifier.citation Matic Jake et al. 2003, 'The pyruvate dehydrogenase complex of Mycoplasma hyopneumoniae contains a novel lipoyl domain arrangement', Elsevier Inc, vol. 319, pp. 99-106. en_US
dc.identifier.issn 0378-1119 en_US
dc.identifier.other C1UNSUBMIT en_US
dc.description.abstract The genes encoding the pyruvate dehydrogenase (PDH) complex (pdhA, pdhB, pdhC and pdhD) from Mycoplasma hyopneumoniae have been cloned and sequenced. The genes are arranged into two operons, designated pdhAB and pdhCD, which are not found together in the chromosome. The pdhA, pdhB, pdhC and pdhD genes encode proteins of predicted molecular masses of 44.2 kDa (pyruvate dehydrogenase major subunit; E1?), 36.6 kDa (pyruvate dehydrogenase minor subunit; E1?), 33.1 kDa (dihydrolipoyl acetyltransferase; E2) and 66.3 kDa (dihydrolipoyl dehydrogenase; E3), respectively. Sequence analysis of the pdhCD operon revealed the presence of a lipoyl-binding domain in pdhD but not in pdhC. The lipoyl domain is believed to act as a ?swinging arm? that spans the gaps between the catalytic domains of each of the subunits. Portions of the N-terminal regions of pdhA and pdhD were expressed as 6?His-tag fusion proteins in Escherichia coli and purified by nickel affinity chromatography. The purified proteins were used to raise antibodies in rabbits, and Western blot analysis was performed with the polyclonal rabbit antiserum. Both the pdhA and pdhD genes were expressed among various strains of M. hyopneumoniae as well as the porcine mycoplasmas, Mycoplasma hyorhinis and Mycoplasma flocculare. Southern hybridisation analysis using probes from pdhA and pdhD detected one copy of each gene in the chromosome of M. hyopneumoniae. Since previous studies have shown pyruvate dehydrogenase activity in M. hyopneumoniae [J. Gen. Microbiol. 134 (1988) 791], it appears likely that a functional lipoyl-binding domain in the N terminus of PdhC is not an absolute prerequisite for pyruvate dehydrogenase enzyme activity. We hypothesise that the lipoyl-binding domain of PdhD is performing the enzymatic function normally attributed to the PdhC lipoyl-binding domain in other organisms. en_US
dc.language en_US
dc.publisher Elsevier Inc en_US
dc.relation.isbasedon en_US
dc.title The pyruvate dehydrogenase complex of Mycoplasma hyopneumoniae contains a novel lipoyl domain arrangement en_US
dc.parent Gene en_US
dc.journal.volume 319 en_US
dc.journal.number en_US
dc.publocation Amsterdam, Netherlands en_US
dc.identifier.startpage 99 en_US
dc.identifier.endpage 106 en_US SCI.Institute for Biotechnology of Infectious Diseases en_US
dc.conference Verified OK en_US
dc.for 060400 en_US
dc.personcode 0000052254 en_US
dc.personcode 0000052255 en_US
dc.personcode 0000052256 en_US
dc.personcode 0000052257 en_US
dc.personcode 0000052258 en_US
dc.personcode 0000035449 en_US
dc.personcode 107126 en_US
dc.percentage 100 en_US Genetics en_US
dc.classification.type FOR-08 en_US
dc.edition en_US
dc.custom en_US en_US
dc.location.activity en_US
dc.description.keywords Mycoplasma hyopneumoniae; Pyruvate dehydrogenase; Lipoyl domain en_US
dc.staffid en_US
dc.staffid 107126 en_US

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