Genes of the HSP70 chaperone family are induced by light. In Chlamydomonas reinhardtii, the induction of HSP70 (70 kDa heat shock protein) chaperones by light results in a partial protection of photosystem II against damage by photoinhibitory conditions. Underexpression of a chloroplast-localized HSP70 protein caused an increased sensitivity of photosystem II to light. Overexpression of this protein had a protective effect. Fluorescence measurements and studies of the turnover of photosystem II core components suggest that this HSP70 might function in both the protection and the regeneration of photosystem II. This concept is supported by fractionation studies in which the plastid HSP70 was found associated with chloroplast membranes. Because the light-induced elevation of HSP70 levels provides protection for photosystem II, we examined whether the chloroplast is involved in this regulation and found that mutants defective in plastid-localized chlorophyll synthesis, i.e. the insertion of Mg2+ into protoporphyrin IX are impaired in the induction of HSP70 by light. Exogenous addition of Mg-protoporphyrin in the dark induced the genes. The combined results support a model in which chlorophyll precursors are essential in the signalling from chloroplast to nucleus that regulates the chaperone genes.

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