Abstract

Cyanobacteria perform oxygenic photosynthesis, and the maintenance of photosynthetic electron transport chains is indispensable to their survival in various environmental conditions. Photosynthetic electron transport in cyanobacteria can be studied through genetic analysis because of the natural competence of cyanobacteria. We here show that a strain overexpressing hik8, a histidine kinase gene related to the circadian clock, exhibits an altered photosynthetic electron transport chain in the unicellular cyanobacterium Synechocystis sp. PCC 6803. Respiratory activity was down-regulated under nitrogen-replete conditions. Photosynthetic activity was slightly lower in the hik8-overexpressing strain than in the wild-type after nitrogen depletion, and the values of photosynthetic parameters were altered by hik8 overexpression under nitrogen-replete and nitrogen-depleted conditions. Transcripts of genes encoding Photosystem I and II were increased by hik8 overexpression under nitrogen-replete conditions. Nitrogen starvation triggers increase in amino acids but the magnitude of the increase in several amino acids was diminished by hik8 overexpression. These genetic data indicate that Hik8 regulates the photosynthetic electron transport, which in turn alters primary metabolism during nitrogen starvation in this cyanobacterium.

Highlights

  • Previous studies showed that Hik8 regulates the expression of genes related to sugar catabolism and the nitrogen-induced sigma factor sigE (Singh and Sherman, 2005; Osanai et al, 2015), and sugar catabolism in Synechocystis 6803 is altered by nitrogen status (Osanai et al, 2006)

  • We examined the involvement of a histidine kinase Hik8 in photosynthetic electron transport, and our genetic analysis revealed that hik8 overexpression modified the expression of PSII and PSI genes (Figures 3–5)

  • Our analysis demonstrated that photosynthetic electron transport is regulated by a circadian-related protein in this cyanobacterium

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Summary

Introduction

Two chlorophyll-binding proteins CP43 and CP47, encoded by psbC and psbB respectively, are included in the reaction center of PSII (Barber, 2014). PsbO, U, and V, are located on the lumenal side of cyanobacterial PSII and function as an oxygenic evolving complex (Barber, 2014). PSI is a large membrane protein complex catalyzing light-driven electron transfer from the soluble electron carrier plastocyanin located on the lumenal side, to ferredoxin, located on the stromal side (Amunts and Nelson, 2009). The central part of the PSI core complex is formed by a heterodimer of the large transmembrane proteins PsaA and PsaB (Amunts and Nelson, 2009). PsaI and PsaL are essential components of a trimer complex in cyanobacteria (Karapetyan et al, 2014)

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