Comparative analyses of exoproteinases produced by three phytopathogenic microorganisms.
Identifieur interne : 001776 ( Main/Exploration ); précédent : 001775; suivant : 001777Comparative analyses of exoproteinases produced by three phytopathogenic microorganisms.
Auteurs : Tatiana A. Valueva [Russie] ; Natalia N. Kudryavtseva ; Alexis V. Sof'In ; Tatiana A. Revina ; Ekaterina L. Gvozdeva ; Elena V. IevlevaSource :
- Journal of pathogens [ 2090-3065 ] ; 2011.
Abstract
Proteinases secreted by the oomycete Phytophthora infestans (Mont.) de Bary, Rhizoctonia solani, and Fusarium culmorum belonging to different families of fungi have been studied to determine if the exoenzyme secretion depends on the environmental conditions and the phylogenetic position of the pathogen. The substrate specificity of the extracellular proteinases of F. culmorum, R. solani, and P. infestans and their sensitivity to the action of synthetic and protein inhibitors suggest that they contain trypsin-like and subtilisin-like enzymes regardless of culture medium composition. The relation of trypsin-like and subtilisin-like enzymes is dependent on the culture medium composition, especially on the form of nitrogen nutrition, particularly in the case of the exoenzymes secreted by R. solani. Phylogenetic analyses have shown that the exoproteinase set of ascomycetes and oomycetes has more similarities than basidiomycetes although they are more distant relatives. Our data suggests that the multiple proteinases secreted by pathogenic fungi could play different roles in pathogenesis, increasing the adaptability and host range, or could have different functions in survival in various ecological habitats outside the host.
DOI: 10.4061/2011/947218
PubMed: 22567343
PubMed Central: PMC3335553
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Comparative analyses of exoproteinases produced by three phytopathogenic microorganisms.</title><author><name sortKey="Valueva, Tatiana A" sort="Valueva, Tatiana A" uniqKey="Valueva T" first="Tatiana A" last="Valueva">Tatiana A. Valueva</name><affiliation wicri:level="1"><nlm:affiliation>A.N. Bach Institute of Biochemistry, Russian Academy of Sciences, Leninsky Prospect 33-2, Moscow 119071, Russia.</nlm:affiliation><country xml:lang="fr">Russie</country><wicri:regionArea>A.N. Bach Institute of Biochemistry, Russian Academy of Sciences, Leninsky Prospect 33-2, Moscow 119071</wicri:regionArea><placeName><settlement type="city">Moscou</settlement><region>District fédéral central</region></placeName></affiliation></author><author><name sortKey="Kudryavtseva, Natalia N" sort="Kudryavtseva, Natalia N" uniqKey="Kudryavtseva N" first="Natalia N" last="Kudryavtseva">Natalia N. Kudryavtseva</name></author><author><name sortKey="Sof In, Alexis V" sort="Sof In, Alexis V" uniqKey="Sof In A" first="Alexis V" last="Sof'In">Alexis V. Sof'In</name></author><author><name sortKey="Revina, Tatiana A" sort="Revina, Tatiana A" uniqKey="Revina T" first="Tatiana A" last="Revina">Tatiana A. Revina</name></author><author><name sortKey="Gvozdeva, Ekaterina L" sort="Gvozdeva, Ekaterina L" uniqKey="Gvozdeva E" first="Ekaterina L" last="Gvozdeva">Ekaterina L. Gvozdeva</name></author><author><name sortKey="Ievleva, Elena V" sort="Ievleva, Elena V" uniqKey="Ievleva E" first="Elena V" last="Ievleva">Elena V. Ievleva</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2011">2011</date><idno type="RBID">pubmed:22567343</idno><idno type="pmid">22567343</idno><idno type="doi">10.4061/2011/947218</idno><idno type="pmc">PMC3335553</idno><idno type="wicri:Area/Main/Corpus">001783</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">001783</idno><idno type="wicri:Area/Main/Curation">001783</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">001783</idno><idno type="wicri:Area/Main/Exploration">001783</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Comparative analyses of exoproteinases produced by three phytopathogenic microorganisms.</title><author><name sortKey="Valueva, Tatiana A" sort="Valueva, Tatiana A" uniqKey="Valueva T" first="Tatiana A" last="Valueva">Tatiana A. Valueva</name><affiliation wicri:level="1"><nlm:affiliation>A.N. Bach Institute of Biochemistry, Russian Academy of Sciences, Leninsky Prospect 33-2, Moscow 119071, Russia.</nlm:affiliation><country xml:lang="fr">Russie</country><wicri:regionArea>A.N. Bach Institute of Biochemistry, Russian Academy of Sciences, Leninsky Prospect 33-2, Moscow 119071</wicri:regionArea><placeName><settlement type="city">Moscou</settlement><region>District fédéral central</region></placeName></affiliation></author><author><name sortKey="Kudryavtseva, Natalia N" sort="Kudryavtseva, Natalia N" uniqKey="Kudryavtseva N" first="Natalia N" last="Kudryavtseva">Natalia N. Kudryavtseva</name></author><author><name sortKey="Sof In, Alexis V" sort="Sof In, Alexis V" uniqKey="Sof In A" first="Alexis V" last="Sof'In">Alexis V. Sof'In</name></author><author><name sortKey="Revina, Tatiana A" sort="Revina, Tatiana A" uniqKey="Revina T" first="Tatiana A" last="Revina">Tatiana A. Revina</name></author><author><name sortKey="Gvozdeva, Ekaterina L" sort="Gvozdeva, Ekaterina L" uniqKey="Gvozdeva E" first="Ekaterina L" last="Gvozdeva">Ekaterina L. Gvozdeva</name></author><author><name sortKey="Ievleva, Elena V" sort="Ievleva, Elena V" uniqKey="Ievleva E" first="Elena V" last="Ievleva">Elena V. Ievleva</name></author></analytic><series><title level="j">Journal of pathogens</title><idno type="eISSN">2090-3065</idno><imprint><date when="2011" type="published">2011</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Proteinases secreted by the oomycete Phytophthora infestans (Mont.) de Bary, Rhizoctonia solani, and Fusarium culmorum belonging to different families of fungi have been studied to determine if the exoenzyme secretion depends on the environmental conditions and the phylogenetic position of the pathogen. The substrate specificity of the extracellular proteinases of F. culmorum, R. solani, and P. infestans and their sensitivity to the action of synthetic and protein inhibitors suggest that they contain trypsin-like and subtilisin-like enzymes regardless of culture medium composition. The relation of trypsin-like and subtilisin-like enzymes is dependent on the culture medium composition, especially on the form of nitrogen nutrition, particularly in the case of the exoenzymes secreted by R. solani. Phylogenetic analyses have shown that the exoproteinase set of ascomycetes and oomycetes has more similarities than basidiomycetes although they are more distant relatives. Our data suggests that the multiple proteinases secreted by pathogenic fungi could play different roles in pathogenesis, increasing the adaptability and host range, or could have different functions in survival in various ecological habitats outside the host.</div></front></TEI><pubmed><MedlineCitation Status="PubMed-not-MEDLINE" Owner="NLM"><PMID Version="1">22567343</PMID><DateCompleted><Year>2012</Year><Month>08</Month><Day>23</Day></DateCompleted><DateRevised><Year>2020</Year><Month>09</Month><Day>29</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">2090-3065</ISSN><JournalIssue CitedMedium="Internet"><Volume>2011</Volume><PubDate><Year>2011</Year></PubDate></JournalIssue><Title>Journal of pathogens</Title><ISOAbbreviation>J Pathog</ISOAbbreviation></Journal><ArticleTitle>Comparative analyses of exoproteinases produced by three phytopathogenic microorganisms.</ArticleTitle><Pagination><MedlinePgn>947218</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.4061/2011/947218</ELocationID><Abstract><AbstractText>Proteinases secreted by the oomycete Phytophthora infestans (Mont.) de Bary, Rhizoctonia solani, and Fusarium culmorum belonging to different families of fungi have been studied to determine if the exoenzyme secretion depends on the environmental conditions and the phylogenetic position of the pathogen. The substrate specificity of the extracellular proteinases of F. culmorum, R. solani, and P. infestans and their sensitivity to the action of synthetic and protein inhibitors suggest that they contain trypsin-like and subtilisin-like enzymes regardless of culture medium composition. The relation of trypsin-like and subtilisin-like enzymes is dependent on the culture medium composition, especially on the form of nitrogen nutrition, particularly in the case of the exoenzymes secreted by R. solani. Phylogenetic analyses have shown that the exoproteinase set of ascomycetes and oomycetes has more similarities than basidiomycetes although they are more distant relatives. Our data suggests that the multiple proteinases secreted by pathogenic fungi could play different roles in pathogenesis, increasing the adaptability and host range, or could have different functions in survival in various ecological habitats outside the host.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Valueva</LastName><ForeName>Tatiana A</ForeName><Initials>TA</Initials><AffiliationInfo><Affiliation>A.N. Bach Institute of Biochemistry, Russian Academy of Sciences, Leninsky Prospect 33-2, Moscow 119071, Russia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Kudryavtseva</LastName><ForeName>Natalia N</ForeName><Initials>NN</Initials></Author><Author ValidYN="Y"><LastName>Sof'in</LastName><ForeName>Alexis V</ForeName><Initials>AV</Initials></Author><Author ValidYN="Y"><LastName>Revina</LastName><ForeName>Tatiana A</ForeName><Initials>TA</Initials></Author><Author ValidYN="Y"><LastName>Gvozdeva</LastName><ForeName>Ekaterina L</ForeName><Initials>EL</Initials></Author><Author ValidYN="Y"><LastName>Ievleva</LastName><ForeName>Elena V</ForeName><Initials>EV</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2011</Year><Month>12</Month><Day>14</Day></ArticleDate></Article><MedlineJournalInfo><Country>Egypt</Country><MedlineTA>J Pathog</MedlineTA><NlmUniqueID>101571433</NlmUniqueID><ISSNLinking>2090-3057</ISSNLinking></MedlineJournalInfo></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2011</Year><Month>06</Month><Day>29</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2011</Year><Month>09</Month><Day>16</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2011</Year><Month>09</Month><Day>21</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2012</Year><Month>5</Month><Day>9</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2011</Year><Month>1</Month><Day>1</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2011</Year><Month>1</Month><Day>1</Day><Hour>0</Hour><Minute>1</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">22567343</ArticleId><ArticleId IdType="doi">10.4061/2011/947218</ArticleId><ArticleId IdType="pmc">PMC3335553</ArticleId></ArticleIdList><ReferenceList><Reference><Citation>Nature. 1970 Aug 15;227(5259):680-5</Citation><ArticleIdList><ArticleId IdType="pubmed">5432063</ArticleId></ArticleIdList></Reference><Reference><Citation>Microbiology. 1999 Oct;145 ( Pt 10):2691-9</Citation><ArticleIdList><ArticleId IdType="pubmed">10537191</ArticleId></ArticleIdList></Reference><Reference><Citation>Science. 2000 Nov 3;290(5493):972-7</Citation><ArticleIdList><ArticleId IdType="pubmed">11062127</ArticleId></ArticleIdList></Reference><Reference><Citation>Biochemistry (Mosc). 2010 Jan;75(1):36-40</Citation><ArticleIdList><ArticleId IdType="pubmed">20331422</ArticleId></ArticleIdList></Reference><Reference><Citation>Biochemistry (Mosc). 2004 Oct;69(10):1092-8</Citation><ArticleIdList><ArticleId IdType="pubmed">15527408</ArticleId></ArticleIdList></Reference><Reference><Citation>Fungal Biol. 2010 Feb-Mar;114(2-3):151-9</Citation><ArticleIdList><ArticleId IdType="pubmed">20960971</ArticleId></ArticleIdList></Reference><Reference><Citation>J Evol Biol. 2004 Nov;17 (6):1204-14</Citation><ArticleIdList><ArticleId IdType="pubmed">15525405</ArticleId></ArticleIdList></Reference><Reference><Citation>PLoS One. 2008 Jun 04;3(6):e2300</Citation><ArticleIdList><ArticleId IdType="pubmed">18523684</ArticleId></ArticleIdList></Reference><Reference><Citation>Microbiology. 1997 Jun;143 ( Pt 6):1983-92</Citation><ArticleIdList><ArticleId IdType="pubmed">9202474</ArticleId></ArticleIdList></Reference><Reference><Citation>Microbiology. 1995 Jan;141 ( Pt 1):1-9</Citation><ArticleIdList><ArticleId IdType="pubmed">7894700</ArticleId></ArticleIdList></Reference><Reference><Citation>Nucleic Acids Res. 2004 Jan 1;32(Database issue):D160-4</Citation><ArticleIdList><ArticleId IdType="pubmed">14681384</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biotechnol. 2007 Feb 1;128(2):297-307</Citation><ArticleIdList><ArticleId IdType="pubmed">17097176</ArticleId></ArticleIdList></Reference><Reference><Citation>Microbiol Mol Biol Rev. 1998 Sep;62(3):597-635</Citation><ArticleIdList><ArticleId IdType="pubmed">9729602</ArticleId></ArticleIdList></Reference><Reference><Citation>Mikrobiologiia. 2006 Nov-Dec;75(6):747-51</Citation><ArticleIdList><ArticleId IdType="pubmed">17205798</ArticleId></ArticleIdList></Reference><Reference><Citation>Anal Biochem. 1980 Feb;102(1):196-202</Citation><ArticleIdList><ArticleId IdType="pubmed">7188842</ArticleId></ArticleIdList></Reference><Reference><Citation>Biokhimiia. 1982 May;47(5):797-802</Citation><ArticleIdList><ArticleId IdType="pubmed">7093382</ArticleId></ArticleIdList></Reference><Reference><Citation>Appl Environ Microbiol. 2000 Jan;66(1):320-4</Citation><ArticleIdList><ArticleId IdType="pubmed">10618242</ArticleId></ArticleIdList></Reference><Reference><Citation>Biochemistry (Mosc). 2000 Jun;65(6):723-7</Citation><ArticleIdList><ArticleId IdType="pubmed">10887294</ArticleId></ArticleIdList></Reference><Reference><Citation>J Gen Microbiol. 1973 Dec;79(2):311-20</Citation><ArticleIdList><ArticleId IdType="pubmed">4589332</ArticleId></ArticleIdList></Reference><Reference><Citation>J Gen Physiol. 1947 Mar 20;30(4):291-310</Citation><ArticleIdList><ArticleId IdType="pubmed">19873496</ArticleId></ArticleIdList></Reference><Reference><Citation>Anal Biochem. 1976 May 7;72:248-54</Citation><ArticleIdList><ArticleId IdType="pubmed">942051</ArticleId></ArticleIdList></Reference><Reference><Citation>FEBS Lett. 1974 Sep 1;45(1):11-3</Citation><ArticleIdList><ArticleId IdType="pubmed">4606338</ArticleId></ArticleIdList></Reference><Reference><Citation>Clin Microbiol Rev. 1999 Jul;12(3):454-500</Citation><ArticleIdList><ArticleId IdType="pubmed">10398676</ArticleId></ArticleIdList></Reference><Reference><Citation>Eukaryot Cell. 2003 Apr;2(2):191-9</Citation><ArticleIdList><ArticleId IdType="pubmed">12684368</ArticleId></ArticleIdList></Reference><Reference><Citation>BMC Evol Biol. 2006 Nov 22;6:99</Citation><ArticleIdList><ArticleId IdType="pubmed">17121679</ArticleId></ArticleIdList></Reference><Reference><Citation>Curr Opin Microbiol. 2002 Oct;5(5):513-9</Citation><ArticleIdList><ArticleId IdType="pubmed">12354560</ArticleId></ArticleIdList></Reference><Reference><Citation>Arch Biochem Biophys. 1961 Nov;95:271-8</Citation><ArticleIdList><ArticleId IdType="pubmed">13890599</ArticleId></ArticleIdList></Reference><Reference><Citation>Mycopathologia. 2004 Feb;157(2):225-31</Citation><ArticleIdList><ArticleId IdType="pubmed">15119860</ArticleId></ArticleIdList></Reference></ReferenceList></PubmedData></pubmed><affiliations><list><country><li>Russie</li></country><region><li>District fédéral central</li></region><settlement><li>Moscou</li></settlement></list><tree><noCountry><name sortKey="Gvozdeva, Ekaterina L" sort="Gvozdeva, Ekaterina L" uniqKey="Gvozdeva E" first="Ekaterina L" last="Gvozdeva">Ekaterina L. Gvozdeva</name><name sortKey="Ievleva, Elena V" sort="Ievleva, Elena V" uniqKey="Ievleva E" first="Elena V" last="Ievleva">Elena V. Ievleva</name><name sortKey="Kudryavtseva, Natalia N" sort="Kudryavtseva, Natalia N" uniqKey="Kudryavtseva N" first="Natalia N" last="Kudryavtseva">Natalia N. Kudryavtseva</name><name sortKey="Revina, Tatiana A" sort="Revina, Tatiana A" uniqKey="Revina T" first="Tatiana A" last="Revina">Tatiana A. Revina</name><name sortKey="Sof In, Alexis V" sort="Sof In, Alexis V" uniqKey="Sof In A" first="Alexis V" last="Sof'In">Alexis V. Sof'In</name></noCountry><country name="Russie"><region name="District fédéral central"><name sortKey="Valueva, Tatiana A" sort="Valueva, Tatiana A" uniqKey="Valueva T" first="Tatiana A" last="Valueva">Tatiana A. Valueva</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Bois/explor/PhytophthoraV1/Data/Main/Exploration
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 001776 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd -nk 001776 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien
|wiki= Bois
|area= PhytophthoraV1
|flux= Main
|étape= Exploration
|type= RBID
|clé= pubmed:22567343
|texte= Comparative analyses of exoproteinases produced by three phytopathogenic microorganisms.
}}
Pour générer des pages wiki
HfdIndexSelect -h $EXPLOR_AREA/Data/Main/Exploration/RBID.i -Sk "pubmed:22567343" \
| HfdSelect -Kh $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd \
| NlmPubMed2Wicri -a PhytophthoraV1
| This area was generated with Dilib version V0.6.38. |  |