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PLANT PHYSIOLOGY , Vol 101, Issue 1 121-126, Copyright © 1993 by American Society of Plant Biologists

METABOLISM AND ENZYMOLOGY

Expression of Escherichia coli Phosphoenolpyruvate Carboxylase in a Cyanobacterium (Functional Complementation of Synechococcus PCC 7942 ppc)

I. Luinenburg and J. R. Coleman
Department of Botany, University of Toronto, Toronto, Ontario, Canada M5S 3B2

The gene (ppc) coding for phosphoenolpyruvate carboxylase (PEPCase) in the cyanobacterium Synechococcus PCC 7942 has been inactivated via insertional mutagenesis while being functionally complemented by Escherichia coli ppc. Cyanobacterial cells functionally complemented by E. coli ppc showed decreased PEPCase activity in crude cell lysates and detergent-permeabilized whole cell assays. Decreased rates of growth, reduced levels of chlorophyll a, and decreased photosynthetic O2 evolution capacity per cell when compared to wild-type cyanobacterial cells were also observed. Phycobiliprotein levels were not affected. The results are discussed in terms of the impact of reduced PEPCase activity on cyanobacterial cell metabolism and the regulatory properties of the E. coli gene product.


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M.-D. Deng and J. R. Coleman
Ethanol Synthesis by Genetic Engineering in Cyanobacteria
Appl. Envir. Microbiol., February 1, 1999; 65(2): 523 - 528.
[Abstract] [Full Text]


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