Plants can accumulate heavy metals when exposed to them at high levels. These metals can interfere with photosynthesis. Limited evidence suggests that increased synthesis of some heat-shock proteins (Hsps) may be a general plant response to metal stress, but the specific functions or structures protected by Hsps remain unidentified. Chloroplast small Hsps (smHsps) protect photosynthetic electron transport (Ph(et)) during heat, oxidative, and photoinhibitory stress, but it is not known if chloroplast smHsps are synthesized during metal stress and protect photosynthesis. Zea mays (corn) plants were exposed to varying soil concentrations of Cu, Ni, Pb, and Zn to determine if chloroplast smHsps are induced by heavy metals, if smHsps protect Ph(et), and any effects on chloroplast smHsp and photosynthesis. Net photosynthesis (Ph(n)) decreased with all metals-more so at higher levels and with longer exposures. Decreases in Ph(n) resulted from damage to photosynthetic metabolism, including Ph(et). All metals increased chloroplast smHsp content, which increased with time of exposure. In vitro, Ph(et) was protected from Pb (but not Ni) by purified chloroplast smHsp added to thylakoids. In vivo, Ph(n) was protected from Ni and Pb by increases in smHsp in a heat-tolerant Agrostis stolonifera selection genotype expressing additional chloroplast smHsps compared to a near-isogenic heat-sensitive genotype. These results are evidence that Hsps protect photosynthesis from heavy metals and are among the first to demonstrate specific functions protected by Hsps during metal stress.

Several types of proteins are known to accumulate as a result of dehydration stress in plants, and many of these are thought to serve a protective function. This includes the dehydrin family of proteins, which accumulate in cells in response to drought, low temperatures, or salinity and in embryo tissues during the maturation phase of seed development, when the seed is losing water in preparation for dormancy. Many studies to date have concentrated on the expression, localization, and function of dehydrins in seed tissues. Our study provides some of the first evidence for a chloroplast-localized dehydrin by using cell fractionation combined with immunofluorescence and immunogold electron microscopy to determine dehydrin location in mature leaf tissues of Pisum sativum and Zea mays. This article also documents constitutive expression of the chloroplast dehydrin as well as expression during different dehydrative stresses. The chloroplast-dehydrin expression pattern differs from most other dehydrins studied to date and suggests a role in basic cell metabolism for this particular dehydrin.