Arps, Peggy J. and Fulton, Gail F. and Minnich, Elizabeth C. and Lidstrom, Mary E. (1993) Genetics of serine pathway enzymes in Methylobacterium extorquens AM1: phosphoenolpyruvate carboxylase and malyl coenzyme A lyase. Journal of Bacteriology, 175 (12). pp. 3776-3783. ISSN 0021-9193 http://resolver.caltech.edu/CaltechAUTHORS:ARPjbact93
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Methylobacterium extorquens AM1 is a facultative methylotrophic bacterium that uses the serine pathway for formaldehyde incorporation as its assimilation pathway during growth on one-carbon compounds. A DNA region from M. extorquens AM1 previously shown to contain genes for the serine pathway enzymes malyl coenzyme A (CoA) lyase and hydroxypyruvate reductase has been characterized in more detail. Insertion mutagenesis revealed an additional region required for growth on one-carbon compounds, and all of the insertion mutants in this region lacked activity for another serine pathway enzyme, the acetyl- CoA-independent phosphoenolpyruvate (PEP) carboxylase. Expression analysis with Escherichia coli of DNA fragments that included the malyl- CoA lyase and PEP carboxylase regions identified five polypeptides, all transcribed in the same direction. Three of these polypeptides were expressed from the region necessary for the acetyl-CoA-independent PEP carboxylase, one was expressed from the region containing the malyl-CoA lyase gene, and the fifth was expressed from a region immediately downstream from the gene encoding hydroxypyruvate reductase. All six genes are transcribed in the same direction, but the transposon insertion data suggest that they are not all cotranscribed.
|Additional Information:||Copyright © 1993, American Society for Microbiology Received 28 December 1992/Accepted 9 April 1993 This work was supported by a grant from the Department of Energy (no. DEFOGO-87ER13753). We thank Stan Tabor for supplying plasmids pGP1-2, pT7-3, pT7-5, and pT7-6.|
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|Deposited On:||13 Feb 2006|
|Last Modified:||26 Dec 2012 08:45|
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