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J Biol Chem, Vol. 275, Issue 1, 167-176, January 7, 2000
From the Department of Biology, University of California,
Santa Cruz, California 95064
By using the process of Repeat-induced Point
mutation (Selker, E. U., and Garrett, P. W. (1988)
Proc. Natl. Acad. Sci. U. S. A. 85, 6870-6874), we
inactivated vma-1, the gene encoding subunit A of the
V-ATPase of Neurospora crassa. Two vma-1 mutant strains were characterized. One was mutated at multiple sites, did not
make a protein product, and produced spores that only rarely
germinated. The other had four point mutations, made a protein product,
and produced viable spores. Neither strain had detectable V-ATPase
activity. The vma-1 mutant strains did not grow in medium
buffered to pH 7.0 or above or in medium supplemented with the cation
Zn2+. They were completely resistant to inhibition by
concanamycin C, supporting our hypothesis that the V-ATPase is the
in vivo target of this antibiotic. Inactivation of the
vma-1 gene had a pronounced effect on morphology and
development of the organism. In the mutants tip growth was inhibited,
and multiple branching was induced. The vma-1 mutant
strains could not differentiate conidia or perithecia. They could grow
slowly as mycelia and could donate nuclei in a sexual cross. A mutation
in the plasma membrane ATPase, which suppressed the sensitivity of wild
type N. crassa to concanamycin, also proved effective in
suppressing the sensitivity of a vma-1 null mutant to basic
pH but did not correct the morphological defects.
Disruption of vma-1, the Gene Encoding the Catalytic
Subunit of the Vacuolar H+-ATPase, Causes Severe
Morphological Changes in Neurospora crassa*
,
*
The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed: Dept. of Biology,
University of California, Santa Cruz, CA 95064. Tel.: 831-459-2245; Fax: 831-459-3139; E-mail: rbowman@biology.ucsc.edu.
Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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