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. 1985 Jul;4(7):1655–1659. doi: 10.1002/j.1460-2075.1985.tb03833.x

Light-dependent degradation of the QB-protein in isolated pea thylakoids

I Ohad 1, D J Kyle 1, J Hirschberg 2
PMCID: PMC554400  PMID: 16453621

Abstract

The 32 000-dalton QB-protein of photosystem II (PS II) is rapidly damaged and removed from isolated pea thylakoids during incubation in the light resulting in a loss of photosynthetic electron flow through PS II. This in vitro photoinhibition is similar to that previously reported with intact Chlamydomonas cells. The damage occurs at a faster rate in vitro, however, due to the inability of isolated thylakoids to synthesize replacement QB-protein. The removal of the damaged QB-protein does not require any soluble components of the chloroplast stroma and is unaffected by the protease inhibitors phenyl-methylsulfonylfluoride or antipain. Unlike the effect of trypsin, no low mol. wt. membrane-bound or soluble fragments of the labelled QB-protein could be identified either by autoradiography or immunologically using polyclonal antibodies specific for the QB-protein. The lightinduced damage to the QB-protein (indicated by a loss of QB functional activity), preceded the removal of the protein from the membrane. We conclude that photodamage of the QB-protein generates a conformational change which renders the protein susceptible to attack by a highly efficient, intrinsic membrane protease.

Keywords: herbicide, photosystem II, protein turnover, quinonebinding, 32 kd

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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