Cutinase and non-specific esterase activities in the conidial mucilage of Colletotrichum graminicola

Detalhes bibliográficos
Autor(a) principal: Pascholati, S. F. [UNESP]
Data de Publicação: 1993
Outros Autores: Deising, H., Leiti, B., Anderson, D., Nicholson, R. L.
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Institucional da UNESP
Texto Completo: http://dx.doi.org/10.1006/pmpp.1993.1004
http://hdl.handle.net/11449/219434
Resumo: Colletotrichum graminicola is the causal agent of anthracnose on a variety of graminaceous monocotyledonous plants, including corn and sorghum. When conidia of C. graminicola are produced in acervuli on infected plant tissues or in culture, they are surrounded by a mucilage. The mucilage, which is composed of high molecular weight glycoproteins, various enzymes, and a self-inhibitor of conidium germination, functions to protect condidia from untimely germination, from desiccation, and from toxic phenolic metabolites produced by the host plant in response to infection. The present investigation demonstrates that the mucilage contains four cutinases whose molecular weights are similar to those of other fungal cutinases. Like other cutinases these enzymes are of the serine-esterase class of hydrolases as shown by inhibition of enzyme activity with diisopropyl fluorophosphate (DIPF). In the presence of high concentrations of DIPF, conidia produced apparently normal, mature appressoria yet were unable to cause disease of corn leaves. The function of the mucilage cutinases is discussed with regard to their importance to the infection process. © 1993 Academic Press, Inc.
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spelling Cutinase and non-specific esterase activities in the conidial mucilage of Colletotrichum graminicolaDIPF, diisopropyl fluorophosphateDPM, disintegrations per minuteColletotrichum graminicola is the causal agent of anthracnose on a variety of graminaceous monocotyledonous plants, including corn and sorghum. When conidia of C. graminicola are produced in acervuli on infected plant tissues or in culture, they are surrounded by a mucilage. The mucilage, which is composed of high molecular weight glycoproteins, various enzymes, and a self-inhibitor of conidium germination, functions to protect condidia from untimely germination, from desiccation, and from toxic phenolic metabolites produced by the host plant in response to infection. The present investigation demonstrates that the mucilage contains four cutinases whose molecular weights are similar to those of other fungal cutinases. Like other cutinases these enzymes are of the serine-esterase class of hydrolases as shown by inhibition of enzyme activity with diisopropyl fluorophosphate (DIPF). In the presence of high concentrations of DIPF, conidia produced apparently normal, mature appressoria yet were unable to cause disease of corn leaves. The function of the mucilage cutinases is discussed with regard to their importance to the infection process. © 1993 Academic Press, Inc.Department of Botany and Plant Pathology Purdue University, West Lafayette, IN 47907-1155Department of Plant Pathology ESALQ/Sao Paulo State University, Piracicaba, SPFäkultat fürBiologie Phytopatologie Universitat Konstanz, Universitatsstrasse 10, YV 7750 KonstanzDepartment of Plant Pathology ESALQ/Sao Paulo State University, Piracicaba, SPPurdue UniversityUniversidade Estadual Paulista (UNESP)Universitat KonstanzPascholati, S. F. [UNESP]Deising, H.Leiti, B.Anderson, D.Nicholson, R. L.2022-04-28T18:55:37Z2022-04-28T18:55:37Z1993-01-01info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/article37-51http://dx.doi.org/10.1006/pmpp.1993.1004Physiological and Molecular Plant Pathology, v. 42, n. 1, p. 37-51, 1993.1096-11780885-5765http://hdl.handle.net/11449/21943410.1006/pmpp.1993.10042-s2.0-38249004946Scopusreponame:Repositório Institucional da UNESPinstname:Universidade Estadual Paulista (UNESP)instacron:UNESPengPhysiological and Molecular Plant Pathologyinfo:eu-repo/semantics/openAccess2022-04-28T18:55:37Zoai:repositorio.unesp.br:11449/219434Repositório InstitucionalPUBhttp://repositorio.unesp.br/oai/requestopendoar:29462022-04-28T18:55:37Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)false
dc.title.none.fl_str_mv Cutinase and non-specific esterase activities in the conidial mucilage of Colletotrichum graminicola
title Cutinase and non-specific esterase activities in the conidial mucilage of Colletotrichum graminicola
spellingShingle Cutinase and non-specific esterase activities in the conidial mucilage of Colletotrichum graminicola
Pascholati, S. F. [UNESP]
DIPF, diisopropyl fluorophosphate
DPM, disintegrations per minute
title_short Cutinase and non-specific esterase activities in the conidial mucilage of Colletotrichum graminicola
title_full Cutinase and non-specific esterase activities in the conidial mucilage of Colletotrichum graminicola
title_fullStr Cutinase and non-specific esterase activities in the conidial mucilage of Colletotrichum graminicola
title_full_unstemmed Cutinase and non-specific esterase activities in the conidial mucilage of Colletotrichum graminicola
title_sort Cutinase and non-specific esterase activities in the conidial mucilage of Colletotrichum graminicola
author Pascholati, S. F. [UNESP]
author_facet Pascholati, S. F. [UNESP]
Deising, H.
Leiti, B.
Anderson, D.
Nicholson, R. L.
author_role author
author2 Deising, H.
Leiti, B.
Anderson, D.
Nicholson, R. L.
author2_role author
author
author
author
dc.contributor.none.fl_str_mv Purdue University
Universidade Estadual Paulista (UNESP)
Universitat Konstanz
dc.contributor.author.fl_str_mv Pascholati, S. F. [UNESP]
Deising, H.
Leiti, B.
Anderson, D.
Nicholson, R. L.
dc.subject.por.fl_str_mv DIPF, diisopropyl fluorophosphate
DPM, disintegrations per minute
topic DIPF, diisopropyl fluorophosphate
DPM, disintegrations per minute
description Colletotrichum graminicola is the causal agent of anthracnose on a variety of graminaceous monocotyledonous plants, including corn and sorghum. When conidia of C. graminicola are produced in acervuli on infected plant tissues or in culture, they are surrounded by a mucilage. The mucilage, which is composed of high molecular weight glycoproteins, various enzymes, and a self-inhibitor of conidium germination, functions to protect condidia from untimely germination, from desiccation, and from toxic phenolic metabolites produced by the host plant in response to infection. The present investigation demonstrates that the mucilage contains four cutinases whose molecular weights are similar to those of other fungal cutinases. Like other cutinases these enzymes are of the serine-esterase class of hydrolases as shown by inhibition of enzyme activity with diisopropyl fluorophosphate (DIPF). In the presence of high concentrations of DIPF, conidia produced apparently normal, mature appressoria yet were unable to cause disease of corn leaves. The function of the mucilage cutinases is discussed with regard to their importance to the infection process. © 1993 Academic Press, Inc.
publishDate 1993
dc.date.none.fl_str_mv 1993-01-01
2022-04-28T18:55:37Z
2022-04-28T18:55:37Z
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv http://dx.doi.org/10.1006/pmpp.1993.1004
Physiological and Molecular Plant Pathology, v. 42, n. 1, p. 37-51, 1993.
1096-1178
0885-5765
http://hdl.handle.net/11449/219434
10.1006/pmpp.1993.1004
2-s2.0-38249004946
url http://dx.doi.org/10.1006/pmpp.1993.1004
http://hdl.handle.net/11449/219434
identifier_str_mv Physiological and Molecular Plant Pathology, v. 42, n. 1, p. 37-51, 1993.
1096-1178
0885-5765
10.1006/pmpp.1993.1004
2-s2.0-38249004946
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv Physiological and Molecular Plant Pathology
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv 37-51
dc.source.none.fl_str_mv Scopus
reponame:Repositório Institucional da UNESP
instname:Universidade Estadual Paulista (UNESP)
instacron:UNESP
instname_str Universidade Estadual Paulista (UNESP)
instacron_str UNESP
institution UNESP
reponame_str Repositório Institucional da UNESP
collection Repositório Institucional da UNESP
repository.name.fl_str_mv Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)
repository.mail.fl_str_mv
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