- THIS ARTICLE
- Full Text (PDF)
- Alert me when this article is cited
- Alert me if a correction is posted
- SERVICES
- Similar articles in this journal
- Similar articles in PubMed
- Alert me to new issues of the journal
- Download to citation manager
- Reprints & Permissions
- CITING ARTICLES
- Citing Articles via HighWire
- Citing Articles via Google Scholar
- GOOGLE SCHOLAR
- Articles by Chary, P.
- Articles by Natvig, D. O.
- Search for Related Content
- PUBMED
- PubMed Citation
- Articles by Chary, P.
- Articles by Natvig, D. O.
Genetics, Vol 137, 723-730, Copyright © 1994
INVESTIGATIONS |
Superoxide Dismutase (sod-1) Null Mutants of Neurospora crassa: Oxidative Stress Sensitivity, Spontaneous Mutation Rate and Response to Mutagens
P. Chary, D. Dillon, A. L. Schroeder and D. O. Natvig
Department of Biology, University of New Mexico, Albuquerque, New Mexico 87131 Present address: Sealy Center for Molecular Science, University of Texas Medical Branch, Galveston, Texas 77555.
Enzymatic superoxide-dismutase activity is believed to be important in defense against the toxic effects of superoxide. Although superoxide dismutases are among the best studied proteins, numerous questions remain concerning the specific biological roles of the various superoxide-dismutase types. In part, this is because the proposed damaging effects of superoxide are manifold, ranging from inactivation of certain metabolic enzymes to DNA damage. Studies with superoxide-deficient mutants have proven valuable, but surprisingly few such studies have been reported. We have constructed and characterized Neurospora crassa mutants that are null for sod-1, the gene that encodes copper-zinc superoxide dismutase. Mutant strains are sensitive to paraquat and elevated oxygen concentrations, and they exhibit an increased spontaneous mutation rate. They appear to have near wild-type sensitivities to near- and far-UV, heat shock and {gamma}-irradiation. Unlike the equivalent Saccharomyces cerevisiae mutant and the sodA sodB double mutant of Escherichia coli, they do not exhibit aerobic auxotrophy. These results are discussed in the context of an attempt to identify consensus phenotypes among superoxide dismutase-deficient mutants. N. crassa sod-1 null mutant strains were also employed in genetic and subcellular fractionation studies. Results support the hypothesis that a single gene (sod-1), located between Fsr-12 and leu-3 on linkage group I, is responsible for most or all CuZn superoxide dismutase activity in this organism.
This article has been cited by other articles:
 |
|
 |
|
  E. H. Smith, R. Janknecht, and L. J. Maher III Succinate inhibition of {alpha}-ketoglutarate-dependent enzymes in a yeast model of paraganglioma Hum. Mol. Genet., December 15, 2007; 16(24): 3136 - 3148. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 N. Mutoh, M. Kawabata, and S. Kitajima Effects of Four Oxidants, Menadione, 1-Chloro-2,4-Dinitrobenzene, Hydrogen Peroxide and Cumene Hydroperoxide, on Fission Yeast Schizosaccharmoyces pombe J. Biochem., December 1, 2005; 138(6): 797 - 804. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 N. S. Park, K. S. Lee, H. D. Sohn, D. H. Kim, S. M. Lee, E. Park, I. Kim, Y. H. Je, and B. R. Jin Molecular cloning, expression, and characterization of the Cu,Zn superoxide dismutase (SOD1) gene from the entomopathogenic fungus Cordyceps militaris Mycologia, January 1, 2005; 97(1): 130 - 138. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 Y. Yoshida and K. Hasunuma Reactive Oxygen Species Affect Photomorphogenesis in Neurospora crassa J. Biol. Chem., February 20, 2004; 279(8): 6986 - 6993. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 S. Michan, F. Lledias, and W. Hansberg Asexual Development Is Increased in Neurospora crassa cat-3-Null Mutant Strains Eukaryot. Cell, August 1, 2003; 2(4): 798 - 808. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 C.-S. Hwang, G.-e. Rhie, J.-H. Oh, W.-K. Huh, H.-S. Yim, and S.-O. Kang Copper- and zinc-containing superoxide dismutase (Cu/ZnSOD) is required for the protection of Candida albicans against oxidative stresses and the expression of its full virulence Microbiology, November 1, 2002; 148(11): 3705 - 3713. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 Q. Yang and K. A. Borkovich Mutational Activation of a G{alpha}i Causes Uncontrolled Proliferation of Aerial Hyphae and Increased Sensitivity to Heat and Oxidative Stress in Neurospora crassa Genetics, January 1, 1999; 151(1): 107 - 117. [Abstract] [Full Text]
|
|
|
|
 |
|
 D. J. Kliebenstein, R.-A. Monde, and R. L. Last Superoxide Dismutase in Arabidopsis: An Eclectic Enzyme Family with Disparate Regulation and Protein Localization Plant Physiology, October 1, 1998; 118(2): 637 - 650. [Abstract] [Full Text]
|
|
|
|
|
|
I. Fridovich Superoxide Anion Radical (Obardot 2), Superoxide Dismutases, and Related Matters J. Biol. Chem., July 25, 1997; 272(30): 18515 - 18517. [Full Text] [PDF]
|
|