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

Autor: Díaz, Eva-María, Sacristán, Mara, Legaz, María-Estrella, Vicente, Carlos
Zdroj: Plant Signaling & Behavior; July 2009, Vol. 4 Issue: 7 p598-603, 6p
Abstrakt: 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 CO2 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 α-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.
Databáze: Supplemental Index