Deletion of PsbM in Tobacco Alters the QB Site Properties and the Electron Flow within Photosystem II

• Published in: The Journal of biological chemistry Vol. 282; no. 13; pp. 9758 - 9767
• Main Authors: Umate, Pavan, Schwenkert, Serena, Karbat, Izhar, Bosco, Cristina Dal, Mlcòchová, Lada, Volz, Stefanie, Zer, Hagit, Herrmann, Reinhold G., Ohad, Itzhak, Meurer, Jörg
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 30.03.2007; American Society for Biochemistry and Molecular Biology
• Subjects: Binding Sites - genetics; Electron Transport - genetics; Gene Deletion; Nicotiana - genetics; Nicotiana - metabolism; Nicotiana - physiology; Photosystem II Protein Complex - genetics; Photosystem II Protein Complex - metabolism; Photosystem II Protein Complex - physiology; Plants, Genetically Modified; Protein Subunits - deficiency; Protein Subunits - genetics; Protein Subunits - metabolism; Quinones - chemistry; Quinones - metabolism
• ISSN: 0021-9258; 1083-351X
• DOI: 10.1074/jbc.M608117200

Photosystem II, the oxygen-evolving complex of photosynthetic organisms, includes an intriguingly large number of low molecular weight polypeptides, including PsbM. Here we describe the first knock-out of psbM using a transplastomic, reverse genetics approach in a higher plant. Homoplastomic ΔpsbM plants exhibit photoautotrophic growth. Biochemical, biophysical, and immunological analyses demonstrate that PsbM is not required for biogenesis of higher order photosystem II complexes. However, photosystem II is highly light-sensitive, and its activity is significantly decreased in ΔpsbM, whereas kinetics of plastid protein synthesis, reassembly of photosystem II, and recovery of its activity are comparable with the wild type. Unlike wild type, phosphorylation of the reaction center proteins D1 and D2 is severely reduced, whereas the redox-controlled phosphorylation of photosystem II light-harvesting complex is reversely regulated in ΔpsbM plants because of accumulation of reduced plastoquinone in the dark and a limited photosystem II-mediated electron transport in the light. Charge recombination in ΔpsbM measured by thermoluminescence oscillations significantly differs from the 2/6 patterns in the wild type. A simulation program of thermoluminescence oscillations indicates a higher QB/Q –B ratio in dark-adapted mutant thylakoids relative to the wild type. The interaction of the QA/QB sites estimated by shifts in the maximal thermoluminescence emission temperature of the Q band, induced by binding of different herbicides to the QB site, is changed indicating alteration of the activation energy for back electron flow. We conclude that PsbM is primarily involved in the interaction of the redox components important for the electron flow within, outward, and backward to photosystem II.