Y. Mellerharel et al., INHIBITION BY POLYPHOSPHATE OF PHYTOPATHOGENIC POLYGALACTURONASES FROM BOTRYTIS-CINEREA, Canadian journal of microbiology, 43(9), 1997, pp. 835-840
Polygalacturonase activity from the phytopathogenic fungus Botrytis ci
nerea was inhibited in vitro by extracellular polyphosphate from Strep
tomyces sp. A50, as well as other polyphosphates of biological and che
mical origin. The extent of inhibition increased with polyphosphate ch
ain length between 20 and 100 P-i residues. Although the activity of p
olygalacturonase from B. cinerea appeared not to depend on the presenc
e of cations, inhibition was partially blocked by divalent cations suc
h as Mg2+ or Ca2+. Production of polyphosphate in Streptomyces sp. A50
was followed by chemical measurements, as well as by in vivo P-31-NMR
analysis. During the first 2 days of growth, polyphosphate accumulate
d within the cells, after which it appeared in the broth as an extrace
llular product. A maximum concentration of extracellular polyphosphate
(1 mM P-i equivalent) was reached, corresponding to about 25% of the
input P-i. NMR analysis suggested that the intracellular form of polyp
hosphate exists as a mobile soluble pool. In contrast, the extracellul
ar form of polyphosphate appears to be complexed with cations.