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Eukaryotic Cell, December 2008, p. 2113-2122, Vol. 7, No. 12
1535-9778/08/$08.00+0 doi:10.1128/EC.00466-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Department of Plant Pathology and Microbiology, 1415 Boyce Hall,1 Institute for Integrative Genome Biology, University of California, Riverside, 900 University Avenue, Riverside, California 925212
Received 31 December 2007/ Accepted 26 September 2008
Mitogen-activated protein kinase (MAPK) signaling cascades are composed of MAPK kinase kinases (MAPKKKs), MAPK kinases (MAPKKs), and MAPKs. In this study, we characterize components of a MAPK cascade in Neurospora crassa (mik-1, MAPKKK; mek-1, MAPKK; and mak-1, MAPK) homologous to that controlling cell wall integrity in Saccharomyces cerevisiae. Growth of basal hyphae is significantly reduced in mik-1, mek-1, and mak-1 deletion mutants on solid medium. All three mutants formed short aerial hyphae and the formation of asexual macroconidia was reduced in
mik-1 mutants and almost abolished in
mek-1 and
mak-1 strains. In contrast, the normally rare asexual spores, arthroconidia, were abundant in cultures of the three mutants.
mik-1,
mek-1, and
mak-1 mutants were unable to form protoperithecia or perithecia when used as females in a sexual cross. The MAK-1 MAPK was not phosphorylated in
mik-1 and
mek-1 mutants, consistent with the involvement of MIK-1, MEK-1, and MAK-1 in the same signaling cascade. Interestingly, we observed increased levels of mRNA and protein for tyrosinase in the mutants under nitrogen starvation, a condition favoring sexual differentiation. Tyrosinase is an enzyme that catalyzes production of the secondary metabolite L-DOPA melanin. These results implicate the MAK-1 pathway in regulation of development and secondary metabolism in filamentous fungi.
Published ahead of print on 10 October 2008.
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