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Greencut Protein CPLD49 of Chlamydomonas Reinhardtii Associates with Thylakoid Membranes and Is Required for Cytochrome B6f Complex Accumulation

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Greencut Protein CPLD49 of Chlamydomonas Reinhardtii Associates with Thylakoid Membranes and Is Required for Cytochrome B6f Complex Accumulation The Plant Journal (2018) 94, 1023–1037 doi: 10.1111/tpj.13915 GreenCut protein CPLD49 of Chlamydomonas reinhardtii associates with thylakoid membranes and is required for cytochrome b6f complex accumulation Tyler M. Wittkopp1,2,† , Shai Saroussi2,† , Wenqiang Yang2 , Xenie Johnson3 , Rick G. Kim1,2 , Mark L. Heinnickel2, James J. Russell1, Witchukorn Phuthong4 , Rachel M. Dent5,6 , Corey D. Broeckling7 , Graham Peers8 , Martin Lohr9 , Francis-Andre Wollman10 , Krishna K. Niyogi5,6 and Arthur R. Grossman2,* 1Department of Biology, Stanford University, Stanford, CA 94305, USA, 2Department of Plant Biology, Carnegie Institution for Science, Stanford, CA 94305, USA, 3Laboratoire de Bioenerg etique et Biotechnologie des Bacteries et Microalgues, CEA Cadarache, Saint Paul lez Durance, France, 4Department of Materials Science and Engineering, Stanford University, Stanford, CA 94305, USA, 5Department of Plant and Microbial Biology, Howard Hughes Medical Institute, University of California, Berkeley, CA 94720- 3102, USA, 6Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA, 7Proteomics and Metabolomics Facility, Colorado State University, Fort Collins, CO 80523, USA, 8Department of Biology, Colorado State University, Fort Collins, CO 80523, USA, 9Institut fur€ Molekulare Physiologie – Pflanzenbiochemie, Johannes Gutenberg-Universitat,€ 55099 Mainz, Germany, and 10Institut de Biologie Physico-Chimique, CNRS-UPMC, Paris, France Received 27 October 2017; revised 23 February 2018; accepted 6 March 2018; published online 30 March 2018. *For correspondence (e-mail [email protected]). †These authors contributed equally to this work. SUMMARY The GreenCut encompasses a suite of nucleus-encoded proteins with orthologs among green lineage organ- isms (plants, green algae), but that are absent or poorly conserved in non-photosynthetic/heterotrophic organisms. In Chlamydomonas reinhardtii, CPLD49 (Conserved in Plant Lineage and Diatoms49) is an uncharacterized GreenCut protein that is critical for maintaining normal photosynthetic function. We demonstrate that a cpld49 mutant has impaired photoautotrophic growth under high-light conditions. The mutant exhibits a nearly 90% reduction in the level of the cytochrome b6f complex (Cytb6f), which impacts linear and cyclic electron transport, but does not compromise the ability of the strain to perform state tran- sitions. Furthermore, CPLD49 strongly associates with thylakoid membranes where it may be part of a membrane protein complex with another GreenCut protein, CPLD38; a mutant null for CPLD38 also impacts Cytb6f complex accumulation. We investigated several potential functions of CPLD49, with some suggested by protein homology. Our findings are congruent with the hypothesis that CPLD38 and CPLD49 are part of a novel thylakoid membrane complex that primarily modulates accumulation, but also impacts the activity of the Cytb6f complex. Based on motifs of CPLD49 and the activities of other CPLD49-like proteins, we suggest a role for this putative dehydrogenase in the synthesis of a lipophilic thylakoid membrane molecule or cofactor that influences the assembly and activity of Cytb6f. Keywords: GreenCut, photosynthesis, cytochrome b6f, electron transport, chloroplast, thylakoid mem- branes, CPLD38, dehydrogenase. INTRODUCTION Oxygenic photosynthesis involves the capture of solar absorbed light to chemical bond energy. Solar energy is energy by thylakoid membrane pigment–protein com- absorbed by light-harvesting complexes I (LHCI) and II plexes and coupled electron transfer reactions that convert (LHCII) that are associated with photosystems I and II (PSI © 2018 The Authors 1023 The Plant Journal © 2018 John Wiley & Sons Ltd 1024 Tyler M. Wittkopp et al. and PSII, respectively) reaction centers. Excited PSII reac- DAC may interact with the PetD subunit of the Cytb6f com- tion centers generate the oxidative environment that plex, the mechanism by which it impacts the levels of the + enables the splitting of water, which liberates O2,H and complex is not understood (Xiao et al., 2012). electrons. The electrons are transferred from PSII to PSI via To identify additional proteins involved in synthesis, the plastoquinone (PQ) pool, the cytochrome b6f complex assembly and stability of photosynthetic complexes, we (Cytb6f) and the mobile electron carrier plastocyanin (PC), examined Chlamydomonas mutants disrupted in genes to ultimately reduce ferredoxin and NADP+, which function encoding various GreenCut proteins. The GreenCut is a as electron donors in anabolic metabolism. This electron bioinformatically derived protein inventory present in transport pathway is known as linear electron flow (LEF). green lineage (photosynthetic) organisms, but absent or In contrast, cyclic electron flow (CEF) involves the transfer poorly conserved in heterotrophic (non-photosynthetic) of electrons in a cycle around PSI. Although CEF does not organisms (Merchant et al., 2007; Karpowicz et al., 2011; generate NADPH, like LEF it is coupled to the establish- Heinnickel and Grossman, 2013; Wittkopp et al., 2016). ment of a transmembrane H+ gradient that drives ATP for- Many GreenCut proteins function within chloroplasts, mation by the chloroplast ATP synthase; both LEF and CEF where they are involved in diverse processes ranging from require Cytb6f. assembly of photosynthetic complexes to influencing elec- Assembly of the photosynthetic machinery involves tron transport and carbon fixation (Schult et al., 2007; coordinated synthesis of nucleus- and chloroplast-encoded Dobakov a et al., 2009; Armbruster et al., 2010; Karamoko polypeptides along with the pigment molecules with which et al., 2011; Kirst et al., 2012; Link et al., 2012; Mininno they associate (Eberhard et al., 2008; Lyska et al., 2013). et al., 2012; Xiao et al., 2012; Calderon et al., 2013; Hein- Recently, several factors necessary for assembly of PSII, nickel et al., 2013, 2016; Fristedt et al., 2014, 2015; Bhuiyan PSI and Cytb6f were identified in cyanobacteria, algae and et al., 2015; Wittkopp et al., 2016). Mutants defective for plants (Rochaix, 2004, 2011; Schottler€ et al., 2011; Chi genes encoding GreenCut proteins have been isolated et al., 2012; Heinnickel et al., 2013, 2016; Nickelsen and using both forward (Dent et al., 2005, 2015) and reverse Rengstl, 2013; Hartings et al., 2017; Wittenberg et al., (Pootakham et al., 2010; Gonzalez-Ballester et al., 2011) 2017). For the unicellular green alga Chlamydomonas rein- genetic screens. In this work, we analyze a Chlamy- hardtii (Chlamydomonas throughout), Cytb6f assembly domonas strain that is unable to synthesize the GreenCut requires a class of proteins that facilitates integration of protein CPLD49, and demonstrate that this protein plays a heme into apocytochrome b6 and apocytochrome f (Inoue critical role in: (i) maintaining normal photosynthetic elec- et al., 1997; Xie et al., 1998; Kuras et al., 2007; Gabilly tron transport; (ii) the accumulation of the Cytb6f complex; et al., 2010; Cline et al., 2017). Many Chlamydomonas and (iii) survival during exposure of cells to HL under pho- mutants have been identified that are defective for the toautotrophic conditions. Furthermore, CPLD49 associates synthesis of Cytb6f, which involves both translational and with thylakoid membranes where it may interact with post-translational control (Kuras and Wollman, 1994; CPLD38, a GreenCut protein also critical for Cytb6f complex Choquet et al., 1998). Interestingly, regulation of transla- accumulation. tion of mRNAs for the chloroplast-encoded Cytb6f subunits operates through a process designated CES (‘controlled by RESULTS epistatic synthesis’; Wollman et al., 1999; Choquet and CPLD49 is necessary for photoautotrophic growth in HL Vallon, 2000; Choquet and Wollman, 2002; Choquet et al., 2003), in which a free subunit of the complex depresses The Chlamydomonas Cre16.g666050 locus encodes translation initiation of the mRNA encoding that subunit. A CPLD49, a GreenCut protein of 448 amino acids with a pre- similar mechanism controls the biogenesis of PSI dicted N-terminal chloroplast transit peptide (Tardiff et al., (Wostrikoff et al., 2004). 2012), two saccharopine dehydrogenase domains (March- We previously identified a thylakoid membrane protein ler-Bauer et al., 2015) and no predicted transmembrane designated CPLD38, which is necessary for proper accumu- sequences (Figure 1a). A partial characterization of the lation of Cytb6f (Heinnickel et al., 2013). The Chlamy- CAL014.01.15 mutant first suggested a critical role for domonas cpld38 mutant accumulates approximately 25% CPLD49 (Cre16.g666050) in photosynthesis (Dent et al., of wild-type (WT) levels of Cytb6f, potentially the conse- 2015). This mutant, which has an insertional disruption in quence of accelerated degradation of this complex. This Cre16.g666050, was described as acetate-requiring, sug- mutant is also sensitive to high light (HL), and has a gesting impairment in photoautotrophic growth (Dent growth defect under photoautotrophic conditions (Hein- et al., 2015). Based on sequence analysis of CAL014.01.15, nickel et al., 2013). An Arabidopsis thaliana (Arabidopsis we determined that the pMS188 cassette (used for random hereafter) mutant lacking the CPLD38 ortholog, designated mutagenesis) was inserted into chromosome 16, creating a DAC (Defective Accumulation of Cytochrome b6f complex), 26 918 bp deletion at the insertion site that completely displayed a similar phenotype (Xiao et al.,
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