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Antisense suppression of the small chloroplast protein CP12 in tobacco: a transcriptional viewpoint.

Plant signaling & behavior (2011-11-25)
Thomas P Howard, Graham J G Upton, Julie C Lloyd, Christine A Raines
RESUMO

The chloroplast protein CP12 forms a multi-enzyme complex with the Calvin-Benson cycle enzymes phosphoribulokinase (PRK) and NADP-glyceraldehyde-3-phosphate dehydrogenase (GAPDH). PRK and GAPDH are inactivated when present in this complex, a process shown in vitro to be dependent upon oxidized CP12. Recently we reported on the importance of CP12 in vivo to higher plant metabolism using antisense suppression of CP12 in tobacco (Nicotiana tabacum). Our results indicated that while only minor changes in photosynthetic carbon fixation and in PRK and GAPDH activities were observed, striking changes in growth rates and morphology were seen. In this article we present data on the transcriptional changes observed in one of the antisense lines and we discuss the major findings in light of the metabolic phenotype described.

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Phosphorylase Kinase from rabbit muscle, lyophilized powder, ≥60 units/mg protein