H. Deising et J. Siegrist, CHITIN DEACETYLASE ACTIVITY OF THE RUST UROMYCES-VICIAE-FABAE IS CONTROLLED BY FUNGAL MORPHOGENESIS, FEMS microbiology letters, 127(3), 1995, pp. 207-211
The broad bean rust fungus Uromyces viciae-fabae exhibits chitin only
on surfaces of those infection structures which in nature are formed o
n the plant cuticle, but not on those differentiated in the intercellu
lar space of the host leaf. Chitin deacetylase, an enzyme which conver
ts chitin to chitosan, has been studied during in vitro differentiatio
n of rust infection structures. Radiometric and gel electrophoretic an
alyses of crude extracts and extracellular washing fluids have shown t
hat chitin deacetylase activity massively increases when the fungus st
arts to penetrate through the stomata, and that formation of the enzym
e is strictly differentiation-specifically controlled. The extracellul
ar portion of chitin deacetylase activity was about 53% in 24-h-old di
fferentiated infection structures. Five isoforms with apparent molecul
ar masses of 48.1, 30.7, 25.2, 15.2 and 12.7 kDa were detectable after
substrate SDS-PAGE. The enzyme is temperature-sensitive and has a pH
optimum of 5.5-6.0.