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J Biol Chem, Vol. 274, Issue 33, 23565-23569, August 13, 1999
From the Henry Hood Research Program, Weis Center for Research,
Pennsylvania State University College of Medicine,
Danville, Pennsylvania 17822 and the Numerous disparate studies in plants, filamentous
fungi, yeast, Archaea, and bacteria have identified one of
the most highly conserved proteins (SNZ family) for which
no function was previously defined. Members have been implicated in the
stress response of plants and yeast and resistance to singlet oxygen
toxicity in the plant pathogen Cercospora. However, it is
found in some anaerobic bacteria and is absent in some aerobic
bacteria. We have cloned the Aspergillus nidulans homologue
(pyroA) of this highly conserved gene and define this gene
family as encoding an enzyme specifically required for pyridoxine
biosynthesis. This realization has enabled us to define a second
pathway for pyridoxine biosynthesis. Some bacteria utilize the
pdx pyridoxine biosynthetic pathway defined in
Escherichia coli and others utilize the
pyroA pathway. However, Eukarya and
Archaea exclusively use the pyroA pathway. We
also found that pyridoxine is destroyed in the presence of singlet oxygen, helping to explain the connection to singlet oxygen sensitivity defined in Cercospora. These data bring clarity to the
previously confusing data on this gene family. However, a new conundrum
now exists; why have highly related bacteria evolved with different pathways for pyridoxine biosynthesis?
The Extremely Conserved pyroA Gene of
Aspergillus nidulans Is Required for Pyridoxine
Synthesis and Is Required Indirectly for Resistance to
Photosensitizers
, and Department of Cell
Biology, Baylor College of Medicine, Houston, Texas 77030
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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