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A more recent version of this article appeared on June 1, 2007
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Submitted on March 23, 2006
Revised on March 6, 2007
Accepted on March 16, 2007
*Department of Plant Pathology and Microbiology and Program in Biochemistry and Molecular Biology, University of California, Riverside, CA 92521; Biology Department, Southwestern Adventist University, Keene, TX 76059
Monitoring Editor: Ralph Isberg
Two-component systems, consisting of proteins with histidine kinase and/or response regulator domains, regulate environmental responses in bacteria, Archaea, fungi, slime molds and plants. Here we characterize RRG-1, a response regulator protein from the filamentous fungus Neurospora crassa. The cell lysis phenotype of 
rrg-1 mutants is reminiscent of osmotic sensitive (os) mutants, including nik-1/os-1 (a histidine kinase) and strains defective in components of a mitogen-activated protein kinase (MAPK) pathway: os-4 (MAPKKK), os-5 (MAPKK) and os-2 (MAPK). Similar to os mutants, rrg-1 strains are sensitive to hyperosmotic conditions and are resistant to the fungicides fludioxonil and iprodione. Like os-5, os-4 and os-2 mutants, but in contrast to nik-1/os-1 strains, rrg-1 mutants do not produce female reproductive structures (protoperithecia) when nitrogen-starved. OS-2-phosphate levels are elevated wild-type cells exposed to NaCl or fludioxonil, but are nearly undetectable in rrg-1 strains. OS-2-phosphate levels are also low in rrg-1, os-2 and os-4 mutants under nitrogen starvation. Analysis of the rrg-1D921N allele, mutated in the predicted phosphorylation site, provides support for phosphorylation-dependent and independent functions for RRG-1. The data support control of vegetative cell integrity, hyperosmotic sensitivity, fungicide resistance and protoperithecial development by RRG-1 through regulation of the OS-4/OS-5/OS-2 MAPK pathway.
These authors contributed equally to this work.
Address correspondence to:
Katherine A. Borkovich (Katherine.Borkovich{at}ucr.edu)
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