IDENTIFICATION OF A GENE-PRODUCT INDUCED BY HARD-SURFACE CONTACT OF COLLETOTRICHUM-GLOEOSPORIOIDES CONIDIA AS A UBIQUITIN-CONJUGATING ENZYME BY YEAST COMPLEMENTATION
Zm. Liu et Pe. Kolattukudy, IDENTIFICATION OF A GENE-PRODUCT INDUCED BY HARD-SURFACE CONTACT OF COLLETOTRICHUM-GLOEOSPORIOIDES CONIDIA AS A UBIQUITIN-CONJUGATING ENZYME BY YEAST COMPLEMENTATION, Journal of bacteriology, 180(14), 1998, pp. 3592-3597
The germinating conidia of many phytopathogenic fungi on hosts must di
fferentiate into an infection structure called the appressorium in ord
er to penetrate their hosts. Chemical signals, such as the host's surf
ace nas or fruit ripening hormone, ethylene, trigger germination and a
ppressorium formation of the avocado pathogen Colletotrichum gloeospor
ioides only after the conidia are in contact with a hard surface, What
role this contact plays is unknown. Here, we describe isolation of ge
nes expressed during the early stage of hard-surface treatment by a di
fferential-display method and report characterization of one of these
cloned genes, chip1 (Colletotrichum hard-surface induced protein 1 gen
e), which encodes a ubiquitin-conjugating enzyme. RNA blots clearly sh
owed that it is induced by hard-surface contact and that ethylene trea
tment enhanced this induction. The predicted open reading frame (ubc1(
Cg)) would encode a 16.2-kDa ubiquitin conjugating enzyme, which shows
82% identity to the Saccharomyces cerevisiae UBC4-UBC5 E2 enzyme, com
prising a major part of total ubiquitin-conjugating activity in stress
ed yeast cells, UBC1(Cg) can complement the proteolysis deficiency of
the S, cerevisiae ubc4 ubc5 mutant, indicating that ubiquitin-dependen
t protein degradation is involved in conidial germination and appresso
rial differentiation.