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J. Bacteriol., Jun 1996, 3044-3048, Vol 178, No. 11
KA Jolley, E Rapaport, DW Hough, MJ Danson, WG Woods and ML Dyall-Smith
The gene encoding dihydrolipoamide dehydrogenase from the halophilic
archaeon, Haloferax volcanii, has been subcloned and overexpressed in the
parent organism by using the halophilic archaeal rRNA promoter. The
recombinant protein has been purified to homogeneity and characterized with
respect to its kinetic, molecular, and salt-dependent properties. A
dihydrolipoamide dehydrogenase-minus mutant of H. volcanii has been created
by homologous recombination with the subcloned gene after insertion of the
mevinolin resistance determinant into the protein- coding region. To
explore the physiological function of the dihydrolipoamide dehydrogenase,
the growth properties of the mutant halophile have been examined.
Copyright © 1996, American Society for Microbiology
Dihydrolipoamide dehydrogenase from the halophilic archaeon Haloferax volcanii: homologous overexpression of the cloned gene
School of Biology and Biochemistry, University of Bath, United Kingdom.
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