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Titolo:
Characterization of mutations in the two-component histidine kinase gene that confer fludioxonil resistance and osmotic sensitivity in the os-1 mutants of Neurospora crassa
Autore:
Ochiai, N; Fujimura, M; Motoyama, T; Ichiishi, A; Usami, R; Horikoshi, K; Yamaguchi, I;
Indirizzi:
Toyo Univ, Fac Life Sci, Itakura 3740193, Japan Toyo Univ Itakura Japan 3740193 iv, Fac Life Sci, Itakura 3740193, Japan Toyo Univ, Dept Engn, Kawagoe, Saitama 3508585, Japan Toyo Univ Kawagoe Saitama Japan 3508585 , Kawagoe, Saitama 3508585, Japan RIKEN Inst, Microbial Toxicol Lab, Wako, Saitama 3510198, Japan RIKEN Inst Wako Saitama Japan 3510198 l Lab, Wako, Saitama 3510198, Japan
Titolo Testata:
PEST MANAGEMENT SCIENCE
fascicolo: 5, volume: 57, anno: 2001,
pagine: 437 - 442
SICI:
1526-498X(200105)57:5<437:COMITT>2.0.ZU;2-F
Fonte:
ISI
Lingua:
ENG
Soggetto:
DICARBOXIMIDE FUNGICIDES; BOTRYTIS-CINEREA; HYPHAL DEVELOPMENT; CANDIDA-ALBICANS; YEAST; FENPICLONIL; SEQUENCES; CASCADE;
Keywords:
dicarboximides; phenylpyrroles; osmotic stress; Neurospora crassa; histidine kinase; two-component signal transduction;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Agriculture,Biology & Environmental Sciences
Citazioni:
31
Recensione:
Indirizzi per estratti:
Indirizzo: Fujimura, M Toyo Univ, Fac Life Sci, Itakura 3740193, Japan Toyo Univ Itakura Japan 3740193 Sci, Itakura 3740193, Japan
Citazione:
N. Ochiai et al., "Characterization of mutations in the two-component histidine kinase gene that confer fludioxonil resistance and osmotic sensitivity in the os-1 mutants of Neurospora crassa", PEST MAN SC, 57(5), 2001, pp. 437-442

Abstract

Osmotic-sensitive (os-1) mutant alleles in Neurospora crassa exhibit resistance to dicarboximides, aromatic hydrocarbons and phenylpyrroles. We have previously reported that the os-1 mutants can be classified into two groupsbased on their resistance to fungicides and osmotic stress: type I, which are highly resistant to iprodione and fludioxonil but moderately sensitive to osmotic stress, and type II, which are highly sensitive to osmotic stress but moderately resistant to fungicides. To explain the mechanism of resistance to these fungicides, we cloned and sequenced the mutant os-1 genes that encode putative osmo-sensing histidine kinase. Within the os-1 gene product (Os1p), the type I strains, NM233t and Y256M209, carried a stop codon at amino acid position 308 and a frameshift at amino acid position 294, respectively. These mutation sites were located on the upstream of histidine kinase and the response regulator domains of Os1p, strongly suggesting that type I strains are null mutants. The null mutants, NM233t and Y256M209, werehighly resistant to iprodione and fludioxonil; thus Os1p is essential for these fungicides to express their antifungal activity. The amino acid changes in Os1p, (625)Pro from Leu, (578)Val from Ala, and (580)Arg from Gly were found in the type II strains, M16, M155-1 and P5990, respectively. Os1p is novel in having six tandem repeats of 90 amino acids in the N terminal. Each amino acid change of the type II strains was located on the fifth unit of six tandem repeats. Type II strains with single amino acid changes were more sensitive to osmotic stress than the null mutants (type I), indicatingthat the amino acid repeats of Os1p were responsible for an important function in osmo-regulation. (C) 2001 Society of Chemical Industry.

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Documento generato il 29/03/20 alle ore 11:24:09