INVESTIGADORES
GALLEGO Susana Mabel
artículos
Título:
20S proteasome and accumulation of oxidized and ubiquitinated proteins in maize leaves subjected to cadmium stress.
Autor/es:
PENA LB; PASQUINI LA; TOMARO ML; GALLEGO SM
Revista:
PHYTOCHEMISTRY
Editorial:
Elsevier
Referencias:
Año: 2007 vol. 68 p. 1139 - 1146
ISSN:
0031-9422
Resumen:
In order to examine the possible
involvement of the 20S proteasome in degradation of oxidized proteins, the effect
of different cadmium concentrations on its activities, protein abundance and
oxidation level were studied using maize (Zea
mays L.) leaf segments. The accumulation of carbonylated and ubiquitinated
proteins was also investigated. Treatment with 50 µM CdCl2 increased
both trypsin and PGPH-like activities of the 20S proteasome. The incremental
changes in 20S proteasome activities were probably caused by an increased level
of 20S proteasome oxidation, with this being responsible for degradation of the
oxidized proteins. When leaf segments were treated with 100 µM CdCl2,
the chymotrysin- and trypsin-like activities of the 20S proteasome also
decreased, with a concomitant increase in accumulation of carbonylated and
ubiquitinated proteins. With both Cd2+ concentrations, the abundance
of the 20S proteasome protein remained similar to the control experiments.
These results provide evidence for the involvement of this proteolytic system
in cadmium-stressed plants.