Loading…

Endopolygalaturonase PG1 in different formae speciales of Fusarium oxysporum

PGI, the major endopolygalacturonase of the vascular wilt pathogen Fusarium oxysporum, was secreted during growth on pectin by 10 of 12 isolates belonging to seven formae speciales, as determined with isoelectric focusing zymograms and sodium dodecyl sulfate-polyacrylamide gel electrophoresis gels....

Full description

Saved in:
Bibliographic Details
Published in:Applied and environmental microbiology 1998-05, Vol.64 (5)
Main Authors: Di Pietro, A. (Universidad de Cardoba, Cordoba, Spain.), Garcia-Maceira, F.I, Huertas-Gonzalez, M.D, Ruiz-Roldan, M.C, Caracuel, Z, Barbieri, A.S, Roncero, M.I.G
Format: Article
Language:English
Subjects:
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
cited_by
cites
container_end_page
container_issue 5
container_start_page
container_title Applied and environmental microbiology
container_volume 64
creator Di Pietro, A. (Universidad de Cardoba, Cordoba, Spain.)
Garcia-Maceira, F.I
Huertas-Gonzalez, M.D
Ruiz-Roldan, M.C
Caracuel, Z
Barbieri, A.S
Roncero, M.I.G
description PGI, the major endopolygalacturonase of the vascular wilt pathogen Fusarium oxysporum, was secreted during growth on pectin by 10 of 12 isolates belonging to seven formae speciales, as determined with isoelectric focusing zymograms and sodium dodecyl sulfate-polyacrylamide gel electrophoresis gels. A Southern analysis of genomic DNA and PCR performed with gene-specific primers revealed that the pg1 locus was highly conserved structurally in most isolates. Two PG1-deficient isolates were identified; one lacked the encoding gene, and the other carried a pg1 allele disrupted by a 3.2-kb insertion with sequence homology to hAT transposases. The virulence for muskmelon of different F. oxysporum f. sp. melonis isolates was not correlated with PG1 production in vitro. We concluded that PG1 is widely distributed in F. oxysporum and that it is not essential for pathogenicity
format article
fullrecord <record><control><sourceid>fao</sourceid><recordid>TN_cdi_fao_agris_US1999000051</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>US1999000051</sourcerecordid><originalsourceid>FETCH-fao_agris_US19990000513</originalsourceid><addsrcrecordid>eNqFzbsKwjAUgOEgCtbLIwh5gcLplWaWVgcHQZ3LwSYlkiYlpwH79jq4O_3DN_wLFiUgqrjIsnLJIgAh4jTNYc02RC8AyKGsInapbedGZ-YeDU7BO4sk-fWUcG15p5WSXtqJK-cHlJxG-dRoJHGneBMIvQ4Dd--ZRufDsGMrhYbk_tctOzT1_XiOFboWe6-pfdwSIcR3D0WS_fMPZd45Tg</addsrcrecordid><sourcetype>Publisher</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype></control><display><type>article</type><title>Endopolygalaturonase PG1 in different formae speciales of Fusarium oxysporum</title><source>American Society for Microbiology Journals</source><source>PubMed Central</source><creator>Di Pietro, A. (Universidad de Cardoba, Cordoba, Spain.) ; Garcia-Maceira, F.I ; Huertas-Gonzalez, M.D ; Ruiz-Roldan, M.C ; Caracuel, Z ; Barbieri, A.S ; Roncero, M.I.G</creator><creatorcontrib>Di Pietro, A. (Universidad de Cardoba, Cordoba, Spain.) ; Garcia-Maceira, F.I ; Huertas-Gonzalez, M.D ; Ruiz-Roldan, M.C ; Caracuel, Z ; Barbieri, A.S ; Roncero, M.I.G</creatorcontrib><description>PGI, the major endopolygalacturonase of the vascular wilt pathogen Fusarium oxysporum, was secreted during growth on pectin by 10 of 12 isolates belonging to seven formae speciales, as determined with isoelectric focusing zymograms and sodium dodecyl sulfate-polyacrylamide gel electrophoresis gels. A Southern analysis of genomic DNA and PCR performed with gene-specific primers revealed that the pg1 locus was highly conserved structurally in most isolates. Two PG1-deficient isolates were identified; one lacked the encoding gene, and the other carried a pg1 allele disrupted by a 3.2-kb insertion with sequence homology to hAT transposases. The virulence for muskmelon of different F. oxysporum f. sp. melonis isolates was not correlated with PG1 production in vitro. We concluded that PG1 is widely distributed in F. oxysporum and that it is not essential for pathogenicity</description><identifier>ISSN: 0099-2240</identifier><identifier>EISSN: 1098-5336</identifier><language>eng</language><subject>ACTIVIDAD ENZIMATICA ; ACTIVITE ENZYMATIQUE ; CUCUMIS MELO ; ENZYMIC ACTIVITY ; FLETRISSEMENT ; FUSARIUM OXYSPORUM ; LOCI ; LOCUS ; MARCHITEZ ; PCR ; POLIGALACTURONASA ; POLYGALACTURONASE ; POLYMERASE CHAIN REACTION ; WILTS</subject><ispartof>Applied and environmental microbiology, 1998-05, Vol.64 (5)</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784</link.rule.ids></links><search><creatorcontrib>Di Pietro, A. (Universidad de Cardoba, Cordoba, Spain.)</creatorcontrib><creatorcontrib>Garcia-Maceira, F.I</creatorcontrib><creatorcontrib>Huertas-Gonzalez, M.D</creatorcontrib><creatorcontrib>Ruiz-Roldan, M.C</creatorcontrib><creatorcontrib>Caracuel, Z</creatorcontrib><creatorcontrib>Barbieri, A.S</creatorcontrib><creatorcontrib>Roncero, M.I.G</creatorcontrib><title>Endopolygalaturonase PG1 in different formae speciales of Fusarium oxysporum</title><title>Applied and environmental microbiology</title><description>PGI, the major endopolygalacturonase of the vascular wilt pathogen Fusarium oxysporum, was secreted during growth on pectin by 10 of 12 isolates belonging to seven formae speciales, as determined with isoelectric focusing zymograms and sodium dodecyl sulfate-polyacrylamide gel electrophoresis gels. A Southern analysis of genomic DNA and PCR performed with gene-specific primers revealed that the pg1 locus was highly conserved structurally in most isolates. Two PG1-deficient isolates were identified; one lacked the encoding gene, and the other carried a pg1 allele disrupted by a 3.2-kb insertion with sequence homology to hAT transposases. The virulence for muskmelon of different F. oxysporum f. sp. melonis isolates was not correlated with PG1 production in vitro. We concluded that PG1 is widely distributed in F. oxysporum and that it is not essential for pathogenicity</description><subject>ACTIVIDAD ENZIMATICA</subject><subject>ACTIVITE ENZYMATIQUE</subject><subject>CUCUMIS MELO</subject><subject>ENZYMIC ACTIVITY</subject><subject>FLETRISSEMENT</subject><subject>FUSARIUM OXYSPORUM</subject><subject>LOCI</subject><subject>LOCUS</subject><subject>MARCHITEZ</subject><subject>PCR</subject><subject>POLIGALACTURONASA</subject><subject>POLYGALACTURONASE</subject><subject>POLYMERASE CHAIN REACTION</subject><subject>WILTS</subject><issn>0099-2240</issn><issn>1098-5336</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1998</creationdate><recordtype>article</recordtype><recordid>eNqFzbsKwjAUgOEgCtbLIwh5gcLplWaWVgcHQZ3LwSYlkiYlpwH79jq4O_3DN_wLFiUgqrjIsnLJIgAh4jTNYc02RC8AyKGsInapbedGZ-YeDU7BO4sk-fWUcG15p5WSXtqJK-cHlJxG-dRoJHGneBMIvQ4Dd--ZRufDsGMrhYbk_tctOzT1_XiOFboWe6-pfdwSIcR3D0WS_fMPZd45Tg</recordid><startdate>199805</startdate><enddate>199805</enddate><creator>Di Pietro, A. (Universidad de Cardoba, Cordoba, Spain.)</creator><creator>Garcia-Maceira, F.I</creator><creator>Huertas-Gonzalez, M.D</creator><creator>Ruiz-Roldan, M.C</creator><creator>Caracuel, Z</creator><creator>Barbieri, A.S</creator><creator>Roncero, M.I.G</creator><scope>FBQ</scope></search><sort><creationdate>199805</creationdate><title>Endopolygalaturonase PG1 in different formae speciales of Fusarium oxysporum</title><author>Di Pietro, A. (Universidad de Cardoba, Cordoba, Spain.) ; Garcia-Maceira, F.I ; Huertas-Gonzalez, M.D ; Ruiz-Roldan, M.C ; Caracuel, Z ; Barbieri, A.S ; Roncero, M.I.G</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-fao_agris_US19990000513</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1998</creationdate><topic>ACTIVIDAD ENZIMATICA</topic><topic>ACTIVITE ENZYMATIQUE</topic><topic>CUCUMIS MELO</topic><topic>ENZYMIC ACTIVITY</topic><topic>FLETRISSEMENT</topic><topic>FUSARIUM OXYSPORUM</topic><topic>LOCI</topic><topic>LOCUS</topic><topic>MARCHITEZ</topic><topic>PCR</topic><topic>POLIGALACTURONASA</topic><topic>POLYGALACTURONASE</topic><topic>POLYMERASE CHAIN REACTION</topic><topic>WILTS</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Di Pietro, A. (Universidad de Cardoba, Cordoba, Spain.)</creatorcontrib><creatorcontrib>Garcia-Maceira, F.I</creatorcontrib><creatorcontrib>Huertas-Gonzalez, M.D</creatorcontrib><creatorcontrib>Ruiz-Roldan, M.C</creatorcontrib><creatorcontrib>Caracuel, Z</creatorcontrib><creatorcontrib>Barbieri, A.S</creatorcontrib><creatorcontrib>Roncero, M.I.G</creatorcontrib><collection>AGRIS</collection><jtitle>Applied and environmental microbiology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Di Pietro, A. (Universidad de Cardoba, Cordoba, Spain.)</au><au>Garcia-Maceira, F.I</au><au>Huertas-Gonzalez, M.D</au><au>Ruiz-Roldan, M.C</au><au>Caracuel, Z</au><au>Barbieri, A.S</au><au>Roncero, M.I.G</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Endopolygalaturonase PG1 in different formae speciales of Fusarium oxysporum</atitle><jtitle>Applied and environmental microbiology</jtitle><date>1998-05</date><risdate>1998</risdate><volume>64</volume><issue>5</issue><issn>0099-2240</issn><eissn>1098-5336</eissn><abstract>PGI, the major endopolygalacturonase of the vascular wilt pathogen Fusarium oxysporum, was secreted during growth on pectin by 10 of 12 isolates belonging to seven formae speciales, as determined with isoelectric focusing zymograms and sodium dodecyl sulfate-polyacrylamide gel electrophoresis gels. A Southern analysis of genomic DNA and PCR performed with gene-specific primers revealed that the pg1 locus was highly conserved structurally in most isolates. Two PG1-deficient isolates were identified; one lacked the encoding gene, and the other carried a pg1 allele disrupted by a 3.2-kb insertion with sequence homology to hAT transposases. The virulence for muskmelon of different F. oxysporum f. sp. melonis isolates was not correlated with PG1 production in vitro. We concluded that PG1 is widely distributed in F. oxysporum and that it is not essential for pathogenicity</abstract></addata></record>
fulltext fulltext
identifier ISSN: 0099-2240
ispartof Applied and environmental microbiology, 1998-05, Vol.64 (5)
issn 0099-2240
1098-5336
language eng
recordid cdi_fao_agris_US1999000051
source American Society for Microbiology Journals; PubMed Central
subjects ACTIVIDAD ENZIMATICA
ACTIVITE ENZYMATIQUE
CUCUMIS MELO
ENZYMIC ACTIVITY
FLETRISSEMENT
FUSARIUM OXYSPORUM
LOCI
LOCUS
MARCHITEZ
PCR
POLIGALACTURONASA
POLYGALACTURONASE
POLYMERASE CHAIN REACTION
WILTS
title Endopolygalaturonase PG1 in different formae speciales of Fusarium oxysporum
url http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-05T00%3A34%3A32IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-fao&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Endopolygalaturonase%20PG1%20in%20different%20formae%20speciales%20of%20Fusarium%20oxysporum&rft.jtitle=Applied%20and%20environmental%20microbiology&rft.au=Di%20Pietro,%20A.%20(Universidad%20de%20Cardoba,%20Cordoba,%20Spain.)&rft.date=1998-05&rft.volume=64&rft.issue=5&rft.issn=0099-2240&rft.eissn=1098-5336&rft_id=info:doi/&rft_dat=%3Cfao%3EUS1999000051%3C/fao%3E%3Cgrp_id%3Ecdi_FETCH-fao_agris_US19990000513%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_id=info:pmid/&rfr_iscdi=true