Linked Life Data

17303450

Source:http://linkedlifedata.com/resource/pubmed/id/17303450

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
8
pubmed:dateCreated
2007-6-5
pubmed:databankReference
pubmed:abstractText
beta-1,6-glucanases degrade the polysaccharide beta-1,6-glucan, a cell wall component in some filamentous fungi. A single copy of a beta-1,6-glucanase gene, designated gcnA, was identified in each of the grass endophytic fungi Neotyphodium lolii and Epichloë festucae. Phylogenetic analysis indicates that the GcnA protein is a member of glycosyl hydrolase family 5, and is closely related to fungal beta-1,6-glucanases implicated in mycoparasitism. The E. festucae gcnA gene was expressed in mycelium grown in culture and in both vegetative and reproductive tissues of perennial ryegrass. A gcnA replacement mutant had reduced beta-1,6-glucanase activity when grown in media containing pustulan as the major carbon source. beta-1,6-glucanase activity was restored in the replacement mutant by introducing multiple copies of the gcnA gene. Growth of DeltagcnA and gcnA-overexpressing strains in vegetative grass tissues was indistinguishable from wild type strains.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
1087-1845
pubmed:author
pubmed:issnType
Print
pubmed:volume
44
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
808-17
pubmed:meshHeading
pubmed:year
2007
pubmed:articleTitle
Functional analysis of a beta-1,6-glucanase gene from the grass endophytic fungus Epichloë festucae.
pubmed:affiliation
Centre for Functional Genomics, Institute of Molecular Biosciences, Massey University, Private Bag 11222, Palmerston North, New Zealand.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't