Linked Life Data

8664505

Source:http://linkedlifedata.com/resource/pubmed/id/8664505

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
1996-8-7
pubmed:databankReference
pubmed:abstractText
Antifungal saponins are produced by many plants and have been implicated as preformed determinants of resistance to fungal attack. The importance of saponin detoxification in fungal pathogenesis has recently been demonstrated for the fungus Gaeumannomyces graminis var. avenae, which produces the enzyme avenacinase. Avenacinase detoxifies the triterpenoid oat root saponin avenacin A-1, and is essential for pathogenicity of G. graminis var.avenae to oats. Here we demonstrate an unexpected relatedness between avenacinase and the tomatinase enzyme produced by Septoria lycopersici (a tomato leaf-infecting fungus), which acts on the steroidal glycoalkaloid alpha-tomatine. The two enzymes share common physicochemical properties and are immunologically cross-reactive; however, there are critical differences in their substrate specificities which reflect the host preferences of the fungi from which the enzymes were purified. The DNA encoding tomatinase was isolated from a S. lycopersici cDNA library using avenacinase DNA as a probe. Comparison of the predicted amino acid sequences of avenacinase and tomatinase revealed that the enzymes are clearly similar.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0894-0282
pubmed:author
pubmed:issnType
Print
pubmed:volume
8
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
971-8
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed:articleTitle
Fungal pathogens of oat roots and tomato leaves employ closely related enzymes to detoxify different host plant saponins.
pubmed:affiliation
Sainsbury Laboratory, John Innes Centre, Norwich, UK.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't