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Stepwise photoinhibition of photosystem II - Studies with Synechocystis species PCC 6803 mutants with a modified D-E loop of the reaction center polypeptide D1
Tekijät: Mulo P, Laakso S, Maenpaa P, Aro EM
Kustantaja: AMER SOC PLANT PHYSIOLOGISTS
Julkaisuvuosi: 1998
Journal: Plant Physiology
Tietokannassa oleva lehden nimi: PLANT PHYSIOLOGY
Lehden akronyymi: PLANT PHYSIOL
Vuosikerta: 117
Numero: 2
Aloitussivu: 483
Lopetussivu: 490
Sivujen määrä: 8
ISSN: 0032-0889
DOI: https://doi.org/10.1104/pp.117.2.483
Tiivistelmä
Several mutant strains of Synechocystis sp. PCC 6803 with large deletions in the D-E loop of the photosystem II (PSII) reaction center polypeptide D1 were subjected to high light to investigate the role of this hydrophilic loop in the photoinhibition cascade of PSII. The tolerance of PSII to photoinhibition in the autotrophic mutant Delta R225-F239 (PD), when oxygen evolution was monitored with 2,6-dichloro-p-benzoquinone and the equal susceptibility compared with control when monitored with bicarbonate, suggested an inactivation of the Q(B)-binding niche as the first event in the photoinhibition cascade in vivo. This step in PD was largely reversible at low light without the need for protein synthesis. Only the next event, inactivation of Q(A) reduction, was irreversible and gave a signal for D1 polypeptide degradation. The heterotrophic deletion mutants Delta G240-V249 and Delta R225-V249 had severely modified Q(B) pockets, yet exhibited high rates of 2,6-dichloro-p-benzoquinone-mediated oxygen evolution and less tolerance to photoinhibition than PD. Moreover, the protein-synthesis-dependent recovery of PSII from photoinhibition was impaired in the Delta G240-V249 and Delta R225-V249 mutants because of the effects of the mutations on the expression of the psbA-2 gene. No specific sequences in the D-E loop were found to be essential for high rates of D1 polypeptide degradation.
Several mutant strains of Synechocystis sp. PCC 6803 with large deletions in the D-E loop of the photosystem II (PSII) reaction center polypeptide D1 were subjected to high light to investigate the role of this hydrophilic loop in the photoinhibition cascade of PSII. The tolerance of PSII to photoinhibition in the autotrophic mutant Delta R225-F239 (PD), when oxygen evolution was monitored with 2,6-dichloro-p-benzoquinone and the equal susceptibility compared with control when monitored with bicarbonate, suggested an inactivation of the Q(B)-binding niche as the first event in the photoinhibition cascade in vivo. This step in PD was largely reversible at low light without the need for protein synthesis. Only the next event, inactivation of Q(A) reduction, was irreversible and gave a signal for D1 polypeptide degradation. The heterotrophic deletion mutants Delta G240-V249 and Delta R225-V249 had severely modified Q(B) pockets, yet exhibited high rates of 2,6-dichloro-p-benzoquinone-mediated oxygen evolution and less tolerance to photoinhibition than PD. Moreover, the protein-synthesis-dependent recovery of PSII from photoinhibition was impaired in the Delta G240-V249 and Delta R225-V249 mutants because of the effects of the mutations on the expression of the psbA-2 gene. No specific sequences in the D-E loop were found to be essential for high rates of D1 polypeptide degradation.
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