Cutinase and non-specific esterase activities in the conidial mucilage of Colletotrichum graminicola
Autor(a) principal: | |
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Data de Publicação: | 1993 |
Outros Autores: | , , , |
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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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:29462024-08-05T20:45:52.373346Repositório 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 |
|
_version_ |
1808129244349333504 |