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@ARTICLE{Vetsch:8363,
author = {Vetsch, M. and Janzik, I. and Schaller, A.},
title = {{C}haracterization of prosystemin expressed in the
baculovirus/insect cell system reveals biological activity
of the systemin precursor},
journal = {Planta},
volume = {211},
issn = {0032-0935},
address = {Berlin},
publisher = {Springer},
reportid = {PreJuSER-8363},
pages = {91 - 97},
year = {2000},
note = {Record converted from VDB: 12.11.2012},
abstract = {Tomato (Lycopersicon esculentum Mill.) prosystemin in
fusion with a viral signal peptide was expressed in Sf21
insect cell cultures after infection with recombinant
baculoviruses. Prosystemin was purified from culture
supernatants and its identity was confirmed by N-terminal
sequence and mass-spectral analyses. Recombinant prosystemin
was found to be equally active as compared to systemin in
inducing the expression of wound-response genes in tomato
plants. In cultured cells of L. peruvianum, prosystemin
elicited a rapid alkalinization of the growth medium. The
timing and dose-dependence of the alkalinization response
were found to be identical for prosystemin and systemin,
respectively. Prosystemin-triggered defense responses were
inhibited by a competitive antagonist of systemin activity,
indicating that the systemin sequence within the primary
structure of prosystemin determines its activity.},
keywords = {J (WoSType)},
cin = {ICG-6},
ddc = {580},
cid = {I:(DE-Juel1)VDB144},
pnm = {Pflanzenphysiologie des Spurengasaustauschs mit der
Atmosphäre},
pid = {G:(DE-Juel1)FUEK82},
shelfmark = {Plant Sciences},
typ = {PUB:(DE-HGF)16},
UT = {WOS:000088156400011},
url = {https://juser.fz-juelich.de/record/8363},
}