1887

Abstract

Methanol dehydrogenase-like protein XoxF of AM1 exhibits a sequence identity of 50 % to the catalytic subunit MxaF of periplasmic methanol dehydrogenase in the same organism. The latter has been characterized in detail, identified as a pyrroloquinoline quinone (PQQ)-dependent protein, and shown to be essential for growth in the presence of methanol in this methylotrophic model bacterium. In contrast, the function of XoxF in AM1 has not yet been elucidated, and a phenotype remained to be described for a mutant. Here, we found that a mutant is less competitive than the wild-type during colonization of the phyllosphere of , indicating a function for XoxF during plant colonization. A comparison of the growth parameters of the AM1 mutant with those of the wild-type during exponential growth revealed a reduced methanol uptake rate and a reduced growth rate for the mutant of about 30 %. Experiments with cells starved for carbon revealed that methanol oxidation in the mutant occurs less rapidly compared with the wild-type, especially in the first minutes after methanol addition. A distinct phenotype for the mutant was also observed when formate and CO production were measured after the addition of methanol or formaldehyde to starved cells. The wild-type, but not the mutant, accumulated formate upon substrate addition and had a 1 h lag in CO production under the experimental conditions. Determination of the kinetic properties of the purified enzyme showed a conversion capacity for both formaldehyde and methanol. The results suggest that XoxF is involved in one-carbon metabolism in AM1.

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2010-08-01
2019-11-13
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