| | A subunit of decaprenyl diphosphate synthase stabilizes octaprenyl diphosphate synthase in Escherichia coli by forming a high-molecular weight complexEdited by Peter Brzezinski Received 11 November 2009; accepted 16 December 2009. published online 04 January 2010. Abstract 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 ispBR321A 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. Department of Applied Bioscience and Biotechnology, Faculty of Life and Environmental Science, Shimane University, Japan  Corresponding author. Address: Faculty of Life and Environmental Science, Shimane University, 1060 Nishikawatsu, Matsue 690-8504, Japan. Fax: +81 852 32 6092.
PII: S0014-5793(09)01075-8 doi:10.1016/j.febslet.2009.12.029 © 2009 Federation of European Biochemical Societies | |
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ABSTRACT
