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The cell recognition model in chlorolichens involving a fungal lectin binding to an algal ligand can be extended to cyanolichens
Author(s) -
Vivas M.,
Sacristán M.,
Legaz M. E.,
Vicente C.
Publication year - 2010
Publication title -
plant biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.871
H-Index - 87
eISSN - 1438-8677
pISSN - 1435-8603
DOI - 10.1111/j.1438-8677.2009.00250.x
Subject(s) - arginase , lectin , biology , nostoc , affinity chromatography , biochemistry , thallus , ligand (biochemistry) , agarose , cell wall , microbiology and biotechnology , botany , enzyme , arginine , bacteria , cyanobacteria , amino acid , receptor , genetics
Leptogium corniculatum , a cyanolichen containing Nostoc as photobiont, produces and secretes arginase to culture medium containing arginine. This secreted arginase was pre‐purified by affinity chromatography on beads of activated agarose to which a polygalactosylated urease, purified from Evernia prunastri , was attached. Arginase was eluted from the beads with 50 m m α‐ d ‐galactose. The eluted arginase binds preferentially to the cell surface of Nostoc isolated from this lichen thallus, although it is also able to bind, to some extent, to the cell surface of the chlorobiont isolated from E. prunastri. Previous studies in chlorolichens have shown that a fungal lectin that develops subsidiary arginase activity can be a factor in recognition of compatible algal cells through binding to a polygalactosylated urease, which acts as a lectin ligand in the algal cell wall. Our experiments demonstrate that this model can now be extended to cyanolichens.