In this study, we investigate the possible role of the FtsH protease, an ATP-dependent zinc metalloprotease, during this process.
First-pass extracted concept
FtsH protease
Candidate: toolkit item1 source documents4 linked claims
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Aliases
FtsH, Thylakoid FtsH protease
Evidence Snippets
Supporting Sources
Linked Claims
Purified FtsH degrades the 23-kD D1 fragment in isolated photosystem II core complexes and in thylakoid membranes depleted of endogenous FtsH.
Quoted textsource-backed
Purified FtsH degraded the 23-kD D1 fragment present in isolated photosystem II core complexes, as well as that in thylakoid membranes depleted of endogenous FtsH.
FtsH is identified as the chloroplast protease acting on the D1 protein during light-induced turnover.
Quoted textsource-backed
In this study, we definitively identify the chloroplast protease acting on the D1 protein during its light-induced turnover.
Degradation of the 23-kD D1 fragment in isolated thylakoids is dependent on ATP hydrolysis and divalent metal ions, suggesting involvement of FtsH protease.
Quoted textsource-backed
The primary light-induced cleavage product of the D1 protein, a 23-kD fragment, was found to be degraded in isolated thylakoids in the dark during a process dependent on ATP hydrolysis and divalent metal ions, suggesting the involvement of FtsH.
The 23-kD D1 fragment is presented as a novel class of FtsH substrate consisting of functionally assembled proteins that have undergone irreversible photooxidative damage and cleavage.
Quoted textsource-backed
the 23-kD D1 fragment represents a novel class of FtsH substrate-functionally assembled proteins that have undergone irreversible photooxidative damage and cleavage.