journal.pone.0050480.pdf 301 KB
Nakagawa, Tomoyuki Faculty of Applied Biological Science, Gifu University
Mitsui, Ryoji Department of Biochemistry, Faculty of Science, Okayama University of Science
Tani, Akio Institute of Plant Science and Resources, Okayama University
Sasa, Kentaro Faculty of Applied Biological Science, Gifu University
Tashiro, Shinya Faculty of Applied Biological Science, Gifu University
Iwama, Tomonori Faculty of Applied Biological Science, Gifu University
Hayakawa, Takashi Faculty of Applied Biological Science, Gifu University
Kawai, Keiichi Tokai Gakuin University
In the methylotrophic bacterium Methylobacterium extorquens strain AM1, MxaF, a Ca2+-dependent methanol dehydrogenase (MDH), is the main enzyme catalyzing methanol oxidation during growth on methanol. The genome of strain AM1 contains another MDH gene homologue, xoxF1, whose function in methanol metabolism has remained unclear. In this work, we show that XoxF1 also functions as an MDH and is La3+-dependent. Despite the absence of Ca2+ in the medium strain AM1 was able to grow on methanol in the presence of La3+. Addition of La3+ increased MDH activity but the addition had no effect on mxaF or xoxF1 expression level. We purified MDH from strain AM1 grown on methanol in the presence of La3+, and its N-terminal amino acid sequence corresponded to that of XoxF1. The enzyme contained La3+ as a cofactor. The ΔmxaF mutant strain could not grow on methanol in the presence of Ca2+, but was able to grow after supplementation with La3+. Taken together, these results show that XoxF1 participates in methanol metabolism as a La3+-dependent MDH in strain AM1.
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PUBLIC LIBRARY SCIENCE
© 2012 Nakagawa et al.
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