Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1-2
pubmed:dateCreated
2005-3-24
pubmed:abstractText
The fungus Venturia inaequalis clone No. 36 isolated from Malus domestica cv. Gloster excretes a melanoprotein of 36 kDa in relatively high amounts during growth in liquid culture. The protein was isolated from the culture medium and purified to homogeneity. It was shown to contain melanin. After raising an antiserum against the isolated protein, the protein could be shown to be located in the apoplast fluid of the V. inaequalis infected Malus domestica cv. Elstar. Partial sequencing of the protein revealed no significant sequence homologies to so far sequenced proteins. The melanoprotein binds ferrous and ferric iron. Moreover, it could be shown that the binding of ferric iron (but not of ferrous iron) leads to a change in the absorbance of the protein suggesting a modification of the protein by ferric, but not by ferrous, iron. In addition to iron, the protein also binds copper, but does not bind manganese or nickel. A possible function of this protein in the recruiting and transport of iron and copper and/or in the protection of the fungus by metal-ion mediated oxidative stress is discussed.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0939-5075
pubmed:author
pubmed:issnType
Print
pubmed:volume
60
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
109-15
pubmed:dateRevised
2009-11-4
pubmed:meshHeading
pubmed:articleTitle
Purification and partial characterization of an extracellular melanoprotein from the fungus Venturia inaequalis.
pubmed:affiliation
Indian Agricultural Research Institute, Biochemistry Division, New Delhi 110012, India.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't