Cellular Localization and Role of Kinase Activity of PMK1 in Magnaporthe grisea

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Published in	Eukaryotic Cell Vol. 3; no. 6; pp. 1525 - 1532
Main Authors	Bruno, Kenneth S., Tenjo, Fernando, Li, Lei, Hamer, John E., Xu, Jin-Rong
Format	Journal Article
Language	English
Published	United States American Society for Microbiology 01.12.2004
Subjects	Alleles Blotting, Western Cell Nucleus - metabolism Fungal Proteins - physiology Gene Deletion Green Fluorescent Proteins - chemistry Green Fluorescent Proteins - metabolism Magnaporthe - enzymology Magnaporthe grisea Mitogen-Activated Protein Kinases - physiology Models, Genetic Mutation Oryza sativa Phosphorylation Promoter Regions, Genetic Recombinant Fusion Proteins - chemistry
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Abstract	Classifications Services EC Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley Reddit StumbleUpon Twitter current issue Spotlights in the Current Issue EC About EC Subscribers Authors Reviewers Advertisers Inquiries from the Press Permissions & Commercial Reprints ASM Journals Public Access Policy EC RSS Feeds 1752 N Street N.W. • Washington DC 20036 202.737.3600 • 202.942.9355 fax • journals@asmusa.org Print ISSN: 1535-9778 Online ISSN: 1535-9786 Copyright © 2014 by the American Society for Microbiology. For an alternate route to EC .asm.org, visit: EC
AbstractList	A mitogen-activated protein (MAP) kinase gene, PMK1 , is known to regulate appressorium formation and infectious hyphal growth in the rice blast fungus Magnaporthe grisea . In this study, we constructed a green fluorescent protein gene- PMK1 fusion (GFP- PMK1 ) to examine the expression and localization of PMK1 in M. grisea during infection-related morphogenesis. The GFP -PMK1 fusion encoded a functional protein that complemented the defect of the pmk1 deletion mutant in appressorium formation and plant infection. Although a weak GFP signal was detectable in vegetative hyphae, conidia, and germ tubes, the expression of GFP-Pmk1 was increased in appressoria and developing conidia. Nuclear localization of GFP-Pmk1 proteins was observed in a certain percentage of appressoria. A kinase-inactive allele and a nonphosphorylatable allele of PMK1 were constructed by site-directed mutagenesis. Expression of these mutant PMK1 alleles did not complement the pmk1 deletion mutant. These data confirm that kinase activity and activation of PMK1 by the upstream MAP kinase kinase are required for appressorium formation and plant infection in M. grisea . When overexpressed with the RP27 promoter in the wild-type strain, both the kinase-inactive and nonphosphorylatable PMK1 fusion proteins caused abnormal germ tube branching. Overexpression of these PMK1 mutant alleles may interfere with the function of native PMK1 during appressorium formation. A mitogen-activated protein (MAP) kinase gene, PMK1, is known to regulate appressorium formation and infectious hyphal growth in the rice blast fungus Magnaporthe grisea. In this study, we constructed a green fluorescent protein gene-PMK1 fusion (GFP-PMK1) to examine the expression and localization of PMK1 in M. grisea during infection-related morphogenesis. The GFP-PMK1 fusion encoded a functional protein that complemented the defect of the pmk1 deletion mutant in appressorium formation and plant infection. Although a weak GFP signal was detectable in vegetative hyphae, conidia, and germ tubes, the expression of GFP-Pmk1 was increased in appressoria and developing conidia. Nuclear localization of GFP-Pmk1 proteins was observed in a certain percentage of appressoria. A kinase-inactive allele and a nonphosphorylatable allele of PMK1 were constructed by site-directed mutagenesis. Expression of these mutant PMK1 alleles did not complement the pmk1 deletion mutant. These data confirm that kinase activity and activation of PMK1 by the upstream MAP kinase kinase are required for appressorium formation and plant infection in M. grisea. When overexpressed with the RP27 promoter in the wild-type strain, both the kinase-inactive and nonphosphorylatable PMK1 fusion proteins caused abnormal germ tube branching. Overexpression of these PMK1 mutant alleles may interfere with the function of native PMK1 during appressorium formation. Classifications Services EC Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley Reddit StumbleUpon Twitter current issue Spotlights in the Current Issue EC About EC Subscribers Authors Reviewers Advertisers Inquiries from the Press Permissions & Commercial Reprints ASM Journals Public Access Policy EC RSS Feeds 1752 N Street N.W. • Washington DC 20036 202.737.3600 • 202.942.9355 fax • journals@asmusa.org Print ISSN: 1535-9778 Online ISSN: 1535-9786 Copyright © 2014 by the American Society for Microbiology. For an alternate route to EC .asm.org, visit: EC A mitogen-activated protein (MAP) kinase gene, PMK1, is known to regulate appressorium formation and infectious hyphal growth in the rice blast fungus Magnaporthe grisea. In this study, we constructed a green fluorescent protein gene-PMK1 fusion (GFP-PMK1) to examine the expression and localization of PMK1 in M. grisea during infection-related morphogenesis. The GFP-PMK1 fusion encoded a functional protein that complemented the defect of the pmk1 deletion mutant in appressorium formation and plant infection. Although a weak GFP signal was detectable in vegetative hyphae, conidia, and germ tubes, the expression of GFP-Pmk1 was increased in appressoria and developing conidia. Nuclear localization of GFP-Pmk1 proteins was observed in a certain percentage of appressoria. A kinase-inactive allele and a nonphosphorylatable allele of PMK1 were constructed by site-directed mutagenesis. Expression of these mutant PMK1 alleles did not complement the pmk1 deletion mutant. These data confirm that kinase activity and activation of PMK1 by the upstream MAP kinase kinase are required for appressorium formation and plant infection in M. grisea. When overexpressed with the RP27 promoter in the wild-type strain, both the kinase-inactive and nonphosphorylatable PMK1 fusion proteins caused abnormal germ tube branching. Overexpression of these PMK1 mutant alleles may interfere with the function of native PMK1 during appressorium formation.A mitogen-activated protein (MAP) kinase gene, PMK1, is known to regulate appressorium formation and infectious hyphal growth in the rice blast fungus Magnaporthe grisea. In this study, we constructed a green fluorescent protein gene-PMK1 fusion (GFP-PMK1) to examine the expression and localization of PMK1 in M. grisea during infection-related morphogenesis. The GFP-PMK1 fusion encoded a functional protein that complemented the defect of the pmk1 deletion mutant in appressorium formation and plant infection. Although a weak GFP signal was detectable in vegetative hyphae, conidia, and germ tubes, the expression of GFP-Pmk1 was increased in appressoria and developing conidia. Nuclear localization of GFP-Pmk1 proteins was observed in a certain percentage of appressoria. A kinase-inactive allele and a nonphosphorylatable allele of PMK1 were constructed by site-directed mutagenesis. Expression of these mutant PMK1 alleles did not complement the pmk1 deletion mutant. These data confirm that kinase activity and activation of PMK1 by the upstream MAP kinase kinase are required for appressorium formation and plant infection in M. grisea. When overexpressed with the RP27 promoter in the wild-type strain, both the kinase-inactive and nonphosphorylatable PMK1 fusion proteins caused abnormal germ tube branching. Overexpression of these PMK1 mutant alleles may interfere with the function of native PMK1 during appressorium formation.
Author	Lei Li Fernando Tenjo Jin-Rong Xu John E. Hamer Kenneth S. Bruno
AuthorAffiliation	Department of Botany and Plant Pathology, 1 Department of Biological Sciences, Purdue University, West Lafayette, Indiana 2
AuthorAffiliation_xml	– name: Department of Botany and Plant Pathology, 1 Department of Biological Sciences, Purdue University, West Lafayette, Indiana 2
Author_xml	– sequence: 1 givenname: Kenneth S. surname: Bruno fullname: Bruno, Kenneth S. organization: Department of Botany and Plant Pathology – sequence: 2 givenname: Fernando surname: Tenjo fullname: Tenjo, Fernando organization: Department of Biological Sciences, Purdue University, West Lafayette, Indiana – sequence: 3 givenname: Lei surname: Li fullname: Li, Lei organization: Department of Botany and Plant Pathology – sequence: 4 givenname: John E. surname: Hamer fullname: Hamer, John E. organization: Department of Biological Sciences, Purdue University, West Lafayette, Indiana – sequence: 5 givenname: Jin-Rong surname: Xu fullname: Xu, Jin-Rong organization: Department of Botany and Plant Pathology
BackLink	https://www.ncbi.nlm.nih.gov/pubmed/15590826$$D View this record in MEDLINE/PubMed
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Notes	ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-1 content type line 23 ObjectType-Article-1 ObjectType-Feature-2 Corresponding author. Mailing address: Department of Botany and Plant Pathology, 915 W. State St., Lilly Hall, Purdue University, West Lafayette, IN 47907. Phone: (765) 496-6918. Fax: (765) 494-0363. E-mail: jinrong@purdue.edu. These authors contributed equally to this work.
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Snippet	Classifications Services EC Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley Reddit... A mitogen-activated protein (MAP) kinase gene, PMK1 , is known to regulate appressorium formation and infectious hyphal growth in the rice blast fungus... A mitogen-activated protein (MAP) kinase gene, PMK1, is known to regulate appressorium formation and infectious hyphal growth in the rice blast fungus...
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SubjectTerms	Alleles Blotting, Western Cell Nucleus - metabolism Fungal Proteins - physiology Gene Deletion Green Fluorescent Proteins - chemistry Green Fluorescent Proteins - metabolism Magnaporthe - enzymology Magnaporthe grisea Mitogen-Activated Protein Kinases - physiology Models, Genetic Mutation Oryza sativa Phosphorylation Promoter Regions, Genetic Recombinant Fusion Proteins - chemistry
Title	Cellular Localization and Role of Kinase Activity of PMK1 in Magnaporthe grisea
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