Detection of trypsin inhibitor in seeds of Eucalyptus urophylla and its influence on the in vitro growth of the fungi Pisolithus tinctorius and Rhizoctonia solani
Autor(a) principal: | |
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Data de Publicação: | 2002 |
Outros Autores: | |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Brazilian Journal of Microbiology |
Texto Completo: | http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1517-83822002000400001 |
Resumo: | Inhibitors of plant proteases can regulate the hydrolysis of proteins inside the cells and also participate in the mechanisms of plant defense against herbivore insects and pathogens. Here, we demonstrated that seeds of Eucalyptus urophylla exhibit activities of trypsin and papain inhibitors, two proteases commonly found in living cells. Low amounts of proteins of the crude protein extract of seeds and fractions partially purified by gel filtration, with inhibitory activity against trypsin, inhibited in vitro the mycelial growth of a compatible isolate of the ectomycorrhizal fungus Pisolithus tinctorius and allowed an unsatisfactory growth of another isolate from Pinus taeda, considered incompatible for this eucalyptus species. The same amounts of inhibitory proteins, when tested in vitro on the pathogen Rhizoctonia solani, did not exhibit any effect on the growth of the pathogen. These results indicate the existence of proteases inhibitors in seeds of E. urophylla which could influence the complex biochemical system that differentiates mechanisms of symbiosis and pathogenicity between plants and microorganisms. |
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Brazilian Journal of Microbiology |
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Detection of trypsin inhibitor in seeds of Eucalyptus urophylla and its influence on the in vitro growth of the fungi Pisolithus tinctorius and Rhizoctonia solaniproteaseinhibitortrypsinPisolithus tinctoriusRhizoctonia solaniInhibitors of plant proteases can regulate the hydrolysis of proteins inside the cells and also participate in the mechanisms of plant defense against herbivore insects and pathogens. Here, we demonstrated that seeds of Eucalyptus urophylla exhibit activities of trypsin and papain inhibitors, two proteases commonly found in living cells. Low amounts of proteins of the crude protein extract of seeds and fractions partially purified by gel filtration, with inhibitory activity against trypsin, inhibited in vitro the mycelial growth of a compatible isolate of the ectomycorrhizal fungus Pisolithus tinctorius and allowed an unsatisfactory growth of another isolate from Pinus taeda, considered incompatible for this eucalyptus species. The same amounts of inhibitory proteins, when tested in vitro on the pathogen Rhizoctonia solani, did not exhibit any effect on the growth of the pathogen. These results indicate the existence of proteases inhibitors in seeds of E. urophylla which could influence the complex biochemical system that differentiates mechanisms of symbiosis and pathogenicity between plants and microorganisms.Sociedade Brasileira de Microbiologia2002-12-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S1517-83822002000400001Brazilian Journal of Microbiology v.33 n.4 2002reponame:Brazilian Journal of Microbiologyinstname:Sociedade Brasileira de Microbiologia (SBM)instacron:SBM10.1590/S1517-83822002000400001info:eu-repo/semantics/openAccessTremacoldi,Célia ReginaPascholati,Sérgio Florentinoeng2014-04-28T00:00:00Zoai:scielo:S1517-83822002000400001Revistahttps://www.scielo.br/j/bjm/ONGhttps://old.scielo.br/oai/scielo-oai.phpbjm@sbmicrobiologia.org.br||mbmartin@usp.br1678-44051517-8382opendoar:2014-04-28T00:00Brazilian Journal of Microbiology - Sociedade Brasileira de Microbiologia (SBM)false |
dc.title.none.fl_str_mv |
Detection of trypsin inhibitor in seeds of Eucalyptus urophylla and its influence on the in vitro growth of the fungi Pisolithus tinctorius and Rhizoctonia solani |
title |
Detection of trypsin inhibitor in seeds of Eucalyptus urophylla and its influence on the in vitro growth of the fungi Pisolithus tinctorius and Rhizoctonia solani |
spellingShingle |
Detection of trypsin inhibitor in seeds of Eucalyptus urophylla and its influence on the in vitro growth of the fungi Pisolithus tinctorius and Rhizoctonia solani Tremacoldi,Célia Regina protease inhibitor trypsin Pisolithus tinctorius Rhizoctonia solani |
title_short |
Detection of trypsin inhibitor in seeds of Eucalyptus urophylla and its influence on the in vitro growth of the fungi Pisolithus tinctorius and Rhizoctonia solani |
title_full |
Detection of trypsin inhibitor in seeds of Eucalyptus urophylla and its influence on the in vitro growth of the fungi Pisolithus tinctorius and Rhizoctonia solani |
title_fullStr |
Detection of trypsin inhibitor in seeds of Eucalyptus urophylla and its influence on the in vitro growth of the fungi Pisolithus tinctorius and Rhizoctonia solani |
title_full_unstemmed |
Detection of trypsin inhibitor in seeds of Eucalyptus urophylla and its influence on the in vitro growth of the fungi Pisolithus tinctorius and Rhizoctonia solani |
title_sort |
Detection of trypsin inhibitor in seeds of Eucalyptus urophylla and its influence on the in vitro growth of the fungi Pisolithus tinctorius and Rhizoctonia solani |
author |
Tremacoldi,Célia Regina |
author_facet |
Tremacoldi,Célia Regina Pascholati,Sérgio Florentino |
author_role |
author |
author2 |
Pascholati,Sérgio Florentino |
author2_role |
author |
dc.contributor.author.fl_str_mv |
Tremacoldi,Célia Regina Pascholati,Sérgio Florentino |
dc.subject.por.fl_str_mv |
protease inhibitor trypsin Pisolithus tinctorius Rhizoctonia solani |
topic |
protease inhibitor trypsin Pisolithus tinctorius Rhizoctonia solani |
description |
Inhibitors of plant proteases can regulate the hydrolysis of proteins inside the cells and also participate in the mechanisms of plant defense against herbivore insects and pathogens. Here, we demonstrated that seeds of Eucalyptus urophylla exhibit activities of trypsin and papain inhibitors, two proteases commonly found in living cells. Low amounts of proteins of the crude protein extract of seeds and fractions partially purified by gel filtration, with inhibitory activity against trypsin, inhibited in vitro the mycelial growth of a compatible isolate of the ectomycorrhizal fungus Pisolithus tinctorius and allowed an unsatisfactory growth of another isolate from Pinus taeda, considered incompatible for this eucalyptus species. The same amounts of inhibitory proteins, when tested in vitro on the pathogen Rhizoctonia solani, did not exhibit any effect on the growth of the pathogen. These results indicate the existence of proteases inhibitors in seeds of E. urophylla which could influence the complex biochemical system that differentiates mechanisms of symbiosis and pathogenicity between plants and microorganisms. |
publishDate |
2002 |
dc.date.none.fl_str_mv |
2002-12-01 |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1517-83822002000400001 |
url |
http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1517-83822002000400001 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
10.1590/S1517-83822002000400001 |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
text/html |
dc.publisher.none.fl_str_mv |
Sociedade Brasileira de Microbiologia |
publisher.none.fl_str_mv |
Sociedade Brasileira de Microbiologia |
dc.source.none.fl_str_mv |
Brazilian Journal of Microbiology v.33 n.4 2002 reponame:Brazilian Journal of Microbiology instname:Sociedade Brasileira de Microbiologia (SBM) instacron:SBM |
instname_str |
Sociedade Brasileira de Microbiologia (SBM) |
instacron_str |
SBM |
institution |
SBM |
reponame_str |
Brazilian Journal of Microbiology |
collection |
Brazilian Journal of Microbiology |
repository.name.fl_str_mv |
Brazilian Journal of Microbiology - Sociedade Brasileira de Microbiologia (SBM) |
repository.mail.fl_str_mv |
bjm@sbmicrobiologia.org.br||mbmartin@usp.br |
_version_ |
1752122199319248896 |