Analysis of covalent flavinylation using thermostable succinate dehydrogenase from Thermus thermophilus and Sulfolobus tokodaii lacking SdhE homologs |
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| Authors: | Asako Kounosu |
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| Affiliation: | Department of Biochemistry and Molecular Biology, Nippon Medical School, Sendagi, Bunkyo-ku, Tokyo 113-8602, Japan |
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| Abstract: | Recent studies have indicated that post-translational flavinylation of succinate dehydrogenase subunit A (SdhA) in eukaryotes and bacteria require the chaperone-like proteins Sdh5 and SdhE, respectively. How does covalent flavinylation occur in prokaryotes, which lack SdhE homologs? In this study, I showed that covalent flavinylation in two hyperthermophilic bacteria/archaea lacking SdhE, Thermus thermophilus and Sulfolobus tokodaii, requires heat and dicarboxylic acid. These thermophilic bacteria/archaea inhabit hot environments and are said to be genetically far removed from mesophilic bacteria which possess SdhE. Since mesophilic bacteria have been effective at covalent bonding in temperate environments, they may have caused the evolution of SdhE. |
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| Keywords: | FAD, flavin adenine dinucleotide FRD, fumarate reductase SDH, succinate dehydrogenase SdhA, SDH subunit A TCA, trichloroacetic acid LB, lysogeny broth PCR, polymerase chain reaction rpm, revolutions per minute bp, base pairs HEPES, 4-(2-hydroxyethyl)-1-piperazineethanesulfonic acid PAGE, polyacrylamide gel electrophoresis SDS, sodium dodecyl sulfate SdhE, succinate dehydrogenase protein E |
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