Abstract

Small CAB-like proteins (SCPs) are single-helix light-harvesting-like proteins found in all organisms performing oxygenic photosynthesis. We investigated the effect of growth in moderate salt stress on these stress-induced proteins in the cyanobacterium Synechocystis sp. PCC 6803 depleted of Photosystem I (PSI), which expresses SCPs constitutively, and compared these cells with a PSI-less/ScpABCDE− mutant. SCPs, by stabilizing chlorophyll-binding proteins and Photosystem II (PSII) assembly, protect PSII from photoinhibitory damages, and in their absence electrons accumulate and will lead to ROS formation. The presence of 0.2 M NaCl in the growth medium increased the respiratory activity and other PSII electron sinks in the PSI-less/ScpABCDE− strain. We postulate that this salt-induced effect consumes the excess of PSII-generated electrons, reduces the pressure of the electron transport chain, and thereby prevents 1O2 production.

Highlights

  • In oxygenic photosynthesis, light energy is used to drive two specialized protein complexes called Photosystem I (PSI) and Photosystem II (PSII), which are embedded in a special membrane system, the thylakoid membrane

  • Cells grown in BG-11 supplemented with NaCl evolved more oxygen; while more than five times ­O2 ­h−1 was produced per cell by the PSIless/ScpABCDE− strain grown in the presence of NaCl (p < 0.001, Table 1), oxygen evolution of the PSI-less culture only slightly increased

  • Proteins were extracted from the same number of cells of the PSI-less/ScpABCDE− and the PSI-less control strain, which had been grown in the presence or absence of NaCl for 4 days

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Summary

Introduction

Light energy is used to drive two specialized protein complexes called Photosystem I (PSI) and Photosystem II (PSII), which are embedded in a special membrane system, the thylakoid membrane. PCC 6803 (hereafter Synechocystis), PQ can be reduced either by PSII or by the NADP(H) dehydrogenase-like complex type I (NDH-1), the succinate dehydrogenase (SDH), and different NDH-2s (Cooley and Vermaas 2001). Electrons are transferred directly from plastoquinol (­PQH2) to the bd quinol oxidases (Cyd; Berry et al 2002) or via Cyt b6f to PSI or an aa3-type cytochrome c oxidase (Cox) complex (Howitt and Vermaas 1998; Ermakova et al 2016). The NDH-1, SDH, and NDH-2 complexes and Cyd are ubiquitous in the thylakoid and the cytoplasmic membranes, while Cox and ARTO have been located only in the thylakoid or cytoplasmic membrane, respectively

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