Ambient pH-regulated enzime secretion in endophytic and pathogenic isolates of the fungal genus Colletotrichum
Autor(a) principal: | |
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Data de Publicação: | 2004 |
Outros Autores: | , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Scientia Agrícola (Online) |
Texto Completo: | http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0103-90162004000300010 |
Resumo: | In fungi a genetic system ensures that enzymes are secreted mainly at ambient pH values corresponding to their optima of activity. Although a great deal of information has been obtained concerning this environmental response, there is a lack of studies involving phytopathogenic, endophytic and entomopathogenic fungi as well as different aspects of fungus-host interactions. This study compares in a plate-clearing assays, the effect of ambient pH in the secretion of amylase, cellulase, lipase, pectinase and protease by endophytic, phytopathogenic, and entomopathogenic isolates belonging to several species of Colletotrichum. All enzymes were secreted in a pH-dependent manner by all isolates. Endophytes and pathogens showed distinct patterns of protease secretion, with optima at alkaline and acid growth conditions, respectively. In liquid medium, a Pi-repressible acid phosphatase of an endophytic isolate responded to ambient pH, having a 14-fold increase in secreted specific activity at acid pH, as compared to alkaline pH. Furthermore, part of a Colletotrichum pacC homologue gene, coding for a transcriptional factor responsible for pH-regulated gene expression, was cloned. Ambient pH seems to be a general factor controlling enzyme secretion in fungus-host interactions through a conserved genetic circuit. |
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Ambient pH-regulated enzime secretion in endophytic and pathogenic isolates of the fungal genus ColletotrichumGlomerellaenzyme secretionendophytespathogenic fungipacCIn fungi a genetic system ensures that enzymes are secreted mainly at ambient pH values corresponding to their optima of activity. Although a great deal of information has been obtained concerning this environmental response, there is a lack of studies involving phytopathogenic, endophytic and entomopathogenic fungi as well as different aspects of fungus-host interactions. This study compares in a plate-clearing assays, the effect of ambient pH in the secretion of amylase, cellulase, lipase, pectinase and protease by endophytic, phytopathogenic, and entomopathogenic isolates belonging to several species of Colletotrichum. All enzymes were secreted in a pH-dependent manner by all isolates. Endophytes and pathogens showed distinct patterns of protease secretion, with optima at alkaline and acid growth conditions, respectively. In liquid medium, a Pi-repressible acid phosphatase of an endophytic isolate responded to ambient pH, having a 14-fold increase in secreted specific activity at acid pH, as compared to alkaline pH. Furthermore, part of a Colletotrichum pacC homologue gene, coding for a transcriptional factor responsible for pH-regulated gene expression, was cloned. Ambient pH seems to be a general factor controlling enzyme secretion in fungus-host interactions through a conserved genetic circuit.Escola Superior de Agricultura "Luiz de Queiroz"2004-06-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S0103-90162004000300010Scientia Agricola v.61 n.3 2004reponame:Scientia Agrícola (Online)instname:Universidade de São Paulo (USP)instacron:USP10.1590/S0103-90162004000300010info:eu-repo/semantics/openAccessMaccheroni Jr.,WalterAraújo,Welington LuizAzevedo,João Lúcioeng2004-07-02T00:00:00Zoai:scielo:S0103-90162004000300010Revistahttp://revistas.usp.br/sa/indexPUBhttps://old.scielo.br/oai/scielo-oai.phpscientia@usp.br||alleoni@usp.br1678-992X0103-9016opendoar:2004-07-02T00:00Scientia Agrícola (Online) - Universidade de São Paulo (USP)false |
dc.title.none.fl_str_mv |
Ambient pH-regulated enzime secretion in endophytic and pathogenic isolates of the fungal genus Colletotrichum |
title |
Ambient pH-regulated enzime secretion in endophytic and pathogenic isolates of the fungal genus Colletotrichum |
spellingShingle |
Ambient pH-regulated enzime secretion in endophytic and pathogenic isolates of the fungal genus Colletotrichum Maccheroni Jr.,Walter Glomerella enzyme secretion endophytes pathogenic fungi pacC |
title_short |
Ambient pH-regulated enzime secretion in endophytic and pathogenic isolates of the fungal genus Colletotrichum |
title_full |
Ambient pH-regulated enzime secretion in endophytic and pathogenic isolates of the fungal genus Colletotrichum |
title_fullStr |
Ambient pH-regulated enzime secretion in endophytic and pathogenic isolates of the fungal genus Colletotrichum |
title_full_unstemmed |
Ambient pH-regulated enzime secretion in endophytic and pathogenic isolates of the fungal genus Colletotrichum |
title_sort |
Ambient pH-regulated enzime secretion in endophytic and pathogenic isolates of the fungal genus Colletotrichum |
author |
Maccheroni Jr.,Walter |
author_facet |
Maccheroni Jr.,Walter Araújo,Welington Luiz Azevedo,João Lúcio |
author_role |
author |
author2 |
Araújo,Welington Luiz Azevedo,João Lúcio |
author2_role |
author author |
dc.contributor.author.fl_str_mv |
Maccheroni Jr.,Walter Araújo,Welington Luiz Azevedo,João Lúcio |
dc.subject.por.fl_str_mv |
Glomerella enzyme secretion endophytes pathogenic fungi pacC |
topic |
Glomerella enzyme secretion endophytes pathogenic fungi pacC |
description |
In fungi a genetic system ensures that enzymes are secreted mainly at ambient pH values corresponding to their optima of activity. Although a great deal of information has been obtained concerning this environmental response, there is a lack of studies involving phytopathogenic, endophytic and entomopathogenic fungi as well as different aspects of fungus-host interactions. This study compares in a plate-clearing assays, the effect of ambient pH in the secretion of amylase, cellulase, lipase, pectinase and protease by endophytic, phytopathogenic, and entomopathogenic isolates belonging to several species of Colletotrichum. All enzymes were secreted in a pH-dependent manner by all isolates. Endophytes and pathogens showed distinct patterns of protease secretion, with optima at alkaline and acid growth conditions, respectively. In liquid medium, a Pi-repressible acid phosphatase of an endophytic isolate responded to ambient pH, having a 14-fold increase in secreted specific activity at acid pH, as compared to alkaline pH. Furthermore, part of a Colletotrichum pacC homologue gene, coding for a transcriptional factor responsible for pH-regulated gene expression, was cloned. Ambient pH seems to be a general factor controlling enzyme secretion in fungus-host interactions through a conserved genetic circuit. |
publishDate |
2004 |
dc.date.none.fl_str_mv |
2004-06-01 |
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=S0103-90162004000300010 |
url |
http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0103-90162004000300010 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
10.1590/S0103-90162004000300010 |
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 |
Escola Superior de Agricultura "Luiz de Queiroz" |
publisher.none.fl_str_mv |
Escola Superior de Agricultura "Luiz de Queiroz" |
dc.source.none.fl_str_mv |
Scientia Agricola v.61 n.3 2004 reponame:Scientia Agrícola (Online) instname:Universidade de São Paulo (USP) instacron:USP |
instname_str |
Universidade de São Paulo (USP) |
instacron_str |
USP |
institution |
USP |
reponame_str |
Scientia Agrícola (Online) |
collection |
Scientia Agrícola (Online) |
repository.name.fl_str_mv |
Scientia Agrícola (Online) - Universidade de São Paulo (USP) |
repository.mail.fl_str_mv |
scientia@usp.br||alleoni@usp.br |
_version_ |
1748936459288576000 |