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Genetics, Vol 137, 791-801, Copyright © 1994
INVESTIGATIONS |
The Drosophila Molybdenum Cofactor Gene cinnamon Is Homologous to Three Escherichia coli Cofactor Proteins and to the Rat Protein Gephyrin
K. P. Kamdar, M. E. Shelton and V. Finnerty
Department of Biology, Emory University, Atlanta, Georgia 30322
Essentially all organisms depend upon molybdenum oxidoreductases which require a molybdopterin cofactor for catalytic activity. Mutations resulting in a lack of the cofactor show a pleiotropic loss of molybdoenzyme activities and thereby define genes involved in cofactor biosynthesis or utilization. In prokaryotes, two operons are directly associated with biosynthesis of the pterin moiety and its side chain while additional loci play a role in the acquisition of molybdenum and/or activation of the cofactor. Here we report the cloning of cinnamon, a Drosophila molybdenum cofactor gene encoding a protein with sequence similarity to three of the prokaryotic cofactor proteins. In addition, the Drosophila cinnamon protein is homologous to gephyrin, a protein isolated from the rat central nervous system. Our results suggest that some portions of the prokaryotic cofactor biosynthetic pathway composed of monofunctional proteins have evolved into a multifunctional protein in higher eukaryotes.
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