Cui, TZ, Kaino, T and Kawamukai, M (2010) A subunit of decaprenyl diphosphate synthase stabilizes octaprenyl diphosphate synthase in Escherichia coli by forming a high-molecular weight complex. FEBS Lett. 584:652-6
The length of the isoprenoid-side chain in ubiquinone, an essential component of the electron transport chain, is defined by poly-prenyl diphosphate synthase, which comprises either homomers (e.g., IspB in Escherichia coli) or heteromers (e.g., decaprenyl diphosphate synthase (Dps1) and D-less polyprenyl diphosphate synthase (Dlp1) in Schizosaccharomyces pombe and in humans). We found that expression of either dlp1 or dps1 recovered the thermo-sensitive growth of an E. coli ispB(R321A) mutant and restored IspB activity and production of Coenzyme Q-8. IspB interacted with Dlp1 (or Dps1), forming a high-molecular weight complex that stabilized IspB, leading to full functionality.
Alkyl and Aryl Transferases/chemistry; Alkyl and Aryl Transferases/genetics; Alkyl and Aryl Transferases/metabolism; Animals; Cell Division; Escherichia coli/enzymology; Escherichia coli/genetics; Escherichia coli/metabolism; Escherichia coli Proteins/chemistry; Escherichia coli Proteins/genetics; Escherichia coli Proteins/metabolism; Genetic Complementation Test; Hot Temperature; Humans; Immunoblotting; Mice; Molecular Weight; Multienzyme Complexes/chemistry; Multienzyme Complexes/metabolism; Mutation; Protein Binding; Protein Subunits/chemistry; Protein Subunits/genetics; Protein Subunits/metabolism; Schizosaccharomyces pombe Proteins/chemistry; Schizosaccharomyces pombe Proteins/genetics; Schizosaccharomyces pombe Proteins/metabolism; Ubiquinone/metabolism
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