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Plant Signal Behav. 2009 Jul;4(7):598-603. Epub 2009 Jul 3.

Isolation and characterization of a cyanobacterium-binding protein and its cell wall receptor in the lichen Peltigera canina.

Author information

1
Laboratory of Plant Physiology, The Lichen Team, Faculty of Biology, Complutense University, Madrid, Spain.

Abstract

Peltigera canina, a cyanolichen containing Nostoc as cyanobiont, produces and secretes arginase to a medium containing arginine. Secreted arginase acts as a lectin by binding to the surface of Nostoc cells through a specific receptor which develops urease activity. The enzyme urease has been located in the cell wall of recently isolated cyanobionts. Cytochemical detection of urease is achieved by producing a black, electron-dense precipitate of cobalt sulfide proceeding from CO(2) evolved from urea hydrolysis in the presence of cobalt chloride. This urease has been pre-purified by affinity chromatography on a bead of active agarose to which arginase was attached. Urease was eluted from the beads by 50 mM alpha-D-galactose. The experimentally probed fact that a fungal lectin developing subsidiary arginase activity acts as a recognition factor of compatible algal cells in chlorolichens can now been expanded to cyanolichens.

PMID:
19820309
PMCID:
PMC2710550
DOI:
10.4161/psb.4.7.9164
[Indexed for MEDLINE]
Free PMC Article

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