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J. Bacteriol., 11 1997, 7098-7102, Vol 179, No. 22
Y Kimura, R Sato, K Mimura and M Sato
A dcm-1 mutant, obtained by transposon mutagenesis of Myxococcus xanthus,
could aggregate and form mounds but was unable to sporulate under nutrient
starvation. A sequence analysis of the site of insertion of the transposon
showed that the insertion lies within the 3' end of a 1,572-bp open reading
frame (ORF) designated the M. xanthus pccB ORF. The wild-type form of the
M. xanthus pccB gene, obtained from a lambdaEMBL library of M. xanthus,
shows extensive similarity to a beta subunit of propionyl coenzyme A (CoA)
carboxylase, an alpha subunit of methylmalonyl-CoA decarboxylase, and a 12S
subunit of transcarboxylase. In enzyme assays, extracts of the dcm-1 mutant
were deficient in propionyl-CoA carboxylase activity. This enzyme catalyzes
the ATP- dependent carboxylation of propionyl-CoA to yield
methylmalonyl-CoA. The methylmalonyl-CoA rescued the dcm-1 mutant fruiting
body and spore development. During development, the dcm-1 mutant cells also
had reduced levels of long-chain fatty acids (C16 to C18) compared to wild-
type cells.
Copyright © 1997, American Society for Microbiology
Propionyl coenzyme A carboxylase is required for development of Myxococcus xanthus
Department of Bioresource Science, Faculty of Agriculture, Kagawa University, Japan. kimura@ag.kagawa-u.ac.jp
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