I. Adamska et al., DEGRADATION OF THE LIGHT-STRESS PROTEIN IS MEDIATED BY AN ATP-INDEPENDENT, SERINE-TYPE PROTEASE UNDER LOW-LIGHT CONDITIONS, European journal of biochemistry, 236(2), 1996, pp. 591-599
Green plants respond to light stress by induction of the light-stress
proteins (ELIPs). These proteins are stable as long as the light stres
s persists but are very rapidly degraded during subsequent low light c
onditions [Adamska, I., Kloppstech, K. & Ohad, I. (1993) J. Biol. Chem
. 268, 5438-5444]. Here we report that the degradation of ELIPs is med
iated by an extrinsic, thylakoid-associated protease which is already
present in the membranes during light stress conditions. Partial purif
ication of the protease by perfusion chromatography indicates that thi
s proteolytic activity may be represented by a protein with an apparen
t molecular mass of 65 kDa. The ELIP-directed protease is localized in
the stroma lamellae of the thylakoid membranes and does not require A
TP or additional stromal factors for proteolysis. The protease has an
optimum activity at pH 7.5-9.5 and requires Mg2+ for its activity. The
ELIP-degrading protease show an unusual temperature sensitivity and b
ecomes reversibly inactivated at temperatures below 20 degrees C and a
bove 30 degrees C. Studies with protease inhibitors indicate that this
enzyme belongs to the serine class of proteases. The enhanced degrada
tion of ELIP in isolated thylakoid membranes after addition of the ion
ophore nigericin suggests that a trans-thylakoid Delta pH or changes i
n ionic strength may be involved in the mechanism of protease activati
on.