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dc.contributor.author
Ten Have, Arjen
dc.contributor.author
Espino, José J.
dc.contributor.author
Dekkers, Ester
dc.contributor.author
Van Sluyter, Steven C.
dc.contributor.author
Brito, Nélida
dc.contributor.author
Kay, John
dc.contributor.author
González, Celedonio
dc.contributor.author
van Kan, Jan A. L.
dc.date.available
2017-02-21T17:25:12Z
dc.date.issued
2010-12
dc.identifier.citation
Ten Have, Arjen; Espino, José J.; Dekkers, Ester; Van Sluyter, Steven C.; Brito, Nélida; et al.; The Botrytis cinerea aspartic proteinase family; Elsevier Inc; Fungal Genetics And Biology; 47; 1; 12-2010; 53-65
dc.identifier.issn
1087-1845
dc.identifier.uri
http://hdl.handle.net/11336/13256
dc.description.abstract
The ascomycete plant pathogen Botrytis cinerea secretes aspartic proteinase (AP) activity. Functional analysis was carried out on five aspartic proteinase genes (Bcap1-5) reported previously. Single and double mutants lacking these five genes showed neither a reduced secreted proteolytic activity, nor a reduction in virulence and they showed no alteration in sensitivity to antifungal proteins purified from grape juice. Scrutiny of the B. cinerea genome revealed the presence of nine additional Bcap genes, denoted Bcap6-14. The product of the Bcap8 gene was found to constitute up to 23% of the total protein secreted by B. cinerea. Bcap8-deficient mutants secreted approximately 70% less AP activity but were just as virulent as the wild-type strain. Phylogenetic analysis showed that Bcap8 has orthologs in many basidiomycetes but only few ascomycetes including the biocontrol fungus Trichoderma harzanium. Potential functions of the 14 APs in B. cinerea are discussed based on their sequence characteristics, phylogeny and predicted localization.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Elsevier Inc
dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
dc.subject
Gray Mould
dc.subject
Bioinformatics
dc.subject
Proteinase
dc.subject
Plant Pathogen
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Phylogeny
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Evolution
dc.subject.classification
Bioquímica y Biología Molecular
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Ciencias Biológicas
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CIENCIAS NATURALES Y EXACTAS
dc.title
The Botrytis cinerea aspartic proteinase family
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2017-02-21T14:38:12Z
dc.journal.volume
47
dc.journal.number
1
dc.journal.pagination
53-65
dc.journal.pais
Países Bajos
dc.journal.ciudad
Amsterdam
dc.description.fil
Fil: Ten Have, Arjen. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Mar del Plata. Instituto de Investigaciones Biológicas; Argentina. Universidad Nacional de Mar del Plata. Facultad de Ciencias Exactas y Naturales; Argentina. Wageningen University. Laboratory of Phytopathology; Países Bajos
dc.description.fil
Fil: Espino, José J.. Universidad de la Laguna; España
dc.description.fil
Fil: Dekkers, Ester. Wageningen University. Laboratory of Phytopathology; Países Bajos
dc.description.fil
Fil: Van Sluyter, Steven C.. The Australian Wine Research Institute; Australia. The University Of Melbourne; Australia
dc.description.fil
Fil: Brito, Nélida. Universidad de la Laguna; España
dc.description.fil
Fil: Kay, John. Cardiff University; Reino Unido
dc.description.fil
Fil: González, Celedonio. Universidad de la Laguna; España
dc.description.fil
Fil: van Kan, Jan A. L.. Wageningen University. Laboratory of Phytopathology; Países Bajos
dc.journal.title
Fungal Genetics And Biology
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S1087184509001765
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1016/j.fgb.2009.10.008
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