We compared by chlorophyll (Chl) fluorescence imaging the effects of two strains of the same virus (Italian and Spanish strains of the Pepper mild mottle virus - PMMoV-I and-S, respectively) in the host plant Nicotiana benthamiana. The infection was visualized either using conventional Chl fluorescence parameters or by an advanced statistical approach, yielding a combinatorial set of images that enhances the contrast between control and PMMoV-infected plants in the early infection steps. Among the conventional Chl fluorescence parameters, the non-photochemical quenching parameter NPQ was found to be an effective PMMoV infection reporter in asymptomatic leaves of N. benthamiana, detecting an intermediate infection phase. The combinatorial imaging revealed the infection earlier than any of the standard Chl fluorescence parameters, detecting the PMMoV-S infection as soon as 4 d post-inoculation (dpi), and PMMoV-I infection at 6 dpi; the delay correlates with the lower virulence of the last viral strain. and M. Pineda ... [et al.].
Some steps in the isolation method of photosystem 2 (PS2)-enriched partícles (BBY) influenced the Cu content of the finál preparation. In particular, the centrifugation at 10 000 X g ušed to remove starch after Triton X-100 treatment of the thylakoids, yielded starch-free BBY with a low copper content. This contrasted with the high Cu content of the starch-containing BBY. Differences in Cu levels of both preparations seemed thus to be related to the starch content of the sample. Four imidentifíed proteins were found in the starch fraction. They are probably new copper binding sites in the photosynthetic cell.
The extrinsic proteins of photosystem II in plants (PsbO, PsbP and PsbQ) are known to be targets of stress. In previous work, differential regulation of hypothetical isoforms of these proteins was observed in Nicotiana benthamiana upon viral infection. Each of these proteins is encoded by a multigene family in this species: there are at least four genes encoding PsbO and PsbP and two encoding PsbQ. The results of structural and functional analyses suggest that PsbO and PsbP isoforms could show differences in activity, based on significant substitutions in their primary structure. Two psbQ sequences were isolated which encode identical mature proteins. and M. I. Pérez-Bueno ... [et al.].