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Thioredoxin-Like2/2-Cys Peroxiredoxin Redox Cascade Supports Oxidative Thiol Modulation in Chloroplasts

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Thioredoxin-Like2/2-Cys Peroxiredoxin Redox Cascade Supports Oxidative Thiol Modulation in Chloroplasts Thioredoxin-like2/2-Cys peroxiredoxin redox cascade supports oxidative thiol modulation in chloroplasts Keisuke Yoshidaa,1, Ayaka Haraa, Kazunori Sugiuraa, Yuki Fukayaa, and Toru Hisaboria,1 aLaboratory for Chemistry and Life Science, Institute of Innovative Research, Tokyo Institute of Technology, Midori-ku, 226-8503 Yokohama, Japan Edited by Bob B. Buchanan, University of California, Berkeley, CA, and approved July 18, 2018 (received for review May 14, 2018) Thiol-based redox regulation is central to adjusting chloroplast characteristics, such as the redox potential and protein surface functions under varying light conditions. A redox cascade via the charge (6–9). Recent studies have revealed the functional diversity ferredoxin-thioredoxin reductase (FTR)/thioredoxin (Trx) pathway of Trx subtypes, as exemplified by their different target selectivities has been well recognized to mediate the light-responsive reduc- (10, 11). tive control of target proteins; however, the molecular basis for In previous work, we studied the diurnal redox behaviors of reoxidizing its targets in the dark remains unidentified. Here, we Trx-targeted proteins in spinach (12) and Arabidopsis (13). Our report a mechanism of oxidative thiol modulation in chloroplasts. results clearly showed that these proteins are sensitively switched We biochemically characterized a chloroplast stroma-localized from oxidized to reduced forms in response to the increase in Arabidopsis atypical Trx from , designated as Trx-like2 (TrxL2). TrxL2 light intensity at dawn, which is indicative of the dynamics of had redox-active properties with an unusually less negative redox chloroplast redox regulation in vivo. These studies also high- potential. By an affinity chromatography-based method, TrxL2 was lighted evidence for another intriguing aspect of chloroplast re- shown to interact with a range of chloroplast redox-regulated pro- teins. The direct discrimination of thiol status indicated that TrxL2 dox regulation; Trx-targeted proteins are reoxidized along with can efficiently oxidize, but not reduce, these proteins. A notable the decrease in light intensity at dusk. This finding raises a exception was found in 2-Cys peroxiredoxin (2CP); TrxL2 was able fundamental question: What triggers the oxidizing reaction? In to reduce 2CP with high efficiency. We achieved a complete in contrast to the FTR/Trx pathway that is responsible for the re- vitro reconstitution of the TrxL2/2CP redox cascade for oxidizing duction process, the molecular basis for oxidative thiol modula- redox-regulated proteins and draining reducing power to hydro- tion has been unidentified. Therefore, this issue can be regarded gen peroxide (H2O2). We further addressed the physiological rel- as a critical gap in the current understanding of chloroplast evance of this system by analyzing protein-oxidation dynamics. redox regulation. In Arabidopsis plants, a decreased level of 2CP led to the impair- In this study, we characterized an atypical Trx from Arabi- ment of the reoxidation of redox-regulated proteins during dopsis, designated as Trx-like2 (TrxL2). A combined set of bio- light–dark transitions. A delayed response of protein reoxidation chemical data indicates that (i) TrxL2 acts as the efficient was concomitant with the prolonged accumulation of reducing oxidation factor of several redox-regulated proteins, and (ii) power in TrxL2. These results suggest an in vivo function of the TrxL2 drains reducing power to 2-Cys peroxiredoxin (2CP) and TrxL2/2CP redox cascade for driving oxidative thiol modulation ultimately to hydrogen peroxide (H2O2). On the basis of protein- in chloroplasts. oxidation dynamics in Arabidopsis plants, we further provide physiological insights into oxidative thiol modulation relying on redox regulation | oxidation | chloroplast | TrxL2 | 2-Cys peroxiredoxin the TrxL2/2CP redox cascade. lant chloroplasts have evolved multiple adaptive strategies Significance Pfor allowing efficient photosynthesis under continuously changing light conditions. Thiol-based redox regulation is a To ensure efficient photosynthetic carbon gain, plant chloro- posttranslational mechanism that plays a major role in the light- plasts have to adjust their own physiology toward changes in responsive control of chloroplast functions. In this regulatory light environments. Specific chloroplast proteins are reversibly system, incident light energy is converted into reducing power by activated–inactivated during light–dark cycles by switching photochemical reactions in thylakoid membrane, which is then the reduction–oxidation states of their Cys residues, which is signaled to redox-regulated target proteins in chloroplasts. The termed redox regulation. A long-standing issue in plant bi- target proteins contain a redox-active Cys pair that forms the ology is the manner in which redox-regulated proteins are disulfide bond in the oxidized state. In most cases, target proteins reoxidized upon the interruption of light exposure. In this are activated upon the reductive cleavage of this bond. Canonical study, we identified the thioredoxin-like2 (TrxL2)/2-Cys per- examples of targets are represented by specific enzymes in the – – oxiredoxin (2CP) redox cascade as a molecular basis for oxi- Calvin Benson cycle (1 3); therefore, chloroplast redox regulation dative thiol modulation in chloroplasts. This finding dissects makes it possible to turn on the CO2 fixation process in concert with the “dark side” of chloroplast redox regulation, providing the excitation of photosynthetic electron transport and, thereby, the an insight into how plants rest their photosynthetic activity light perception. at night. It has been firmly established by earlier pioneering studies that the ferredoxin-thioredoxin reductase (FTR)/thioredoxin (Trx) Author contributions: K.Y. and T.H. designed research; K.Y., A.H., K.S., and Y.F. performed pathway serves to transfer reducing power from the electron research; K.Y., K.S., and T.H. analyzed data; and K.Y. and T.H. wrote the paper. transport chain to the target proteins (1, 2). The soluble [4Fe-4S] The authors declare no conflict of interest. protein FTR receives reducing power from photosynthetically This article is a PNAS Direct Submission. reduced ferredoxin and supplies it to Trx (4, 5). Trx is a small Published under the PNAS license. ubiquitous protein with a conserved WCGPC motif in its active 1To whom correspondence may be addressed. Email: [email protected] or site. The reduced form of Trx provides reducing power to target [email protected]. proteins via a dithiol–disulfide exchange reaction, thereby modu- This article contains supporting information online at www.pnas.org/lookup/suppl/doi:10. lating the enzymatic activity of targets. Chloroplasts harbor five 1073/pnas.1808284115/-/DCSupplemental. subtypes of Trx (f, m, x, y,andz), which have distinct molecular Published online August 13, 2018. E8296–E8304 | PNAS | vol. 115 | no. 35 www.pnas.org/cgi/doi/10.1073/pnas.1808284115 Downloaded by guest on September 28, 2021 Results TrxL2 Has a Cross-Talk with Various Redox-Regulated Proteins. We TrxL2 Is Localized to Chloroplast Stroma. Genomic and phylogenic explored TrxL2-interacting proteins in chloroplasts. To this end, studies have identified multiple Trx-like proteins in plants (14); we applied an affinity chromatography-based screening method however, their biochemical or physiological characteristics re- (18) using TrxL2 monocysteinic mutants (TrxL2CS) as bait. main largely unclear. In this study, we noted one type of Trx-like Chloroplast soluble proteins extracted from spinach leaves were proteins possessing a putative active site motif of WCRKC (SI loaded onto a TrxL2CS-immobilized affinity chromatography Appendix, Fig. S1). This atypical Trx motif is marked by two column. Proteins associated with TrxL2CS via the mixed-disulfide bond were eluted by DTT and then identified using mass spec- positively charged hydrophilic amino acids (Arg and Lys) be- trometry (SI Appendix, Fig. S5A). Some proteins, including tween the Cys residues. This protein was previously termed Rubisco activase (RCA) and 2CP, were identified as possible WCRKC Trx (15) or TrxL2 (14); we adopted the latter name in TrxL2-interacting partners. Further analyses of protein elu- this study. tion patterns by immunoblotting indicated that fructose-1,6- In Arabidopsis, TrxL2 is encoded by two genes (At5g06690 for bisphosphatase (FBPase), sedoheptulose-1,7-bisphosphatase TrxL2.1 and At5g04260 for TrxL2.2) (SI Appendix, Fig. S1). Both (SBPase), NADP-malate dehydrogenase (NADP-MDH), ADP- isoforms have been previously shown to be targeted to chloro- glucose pyrophosphorylase (AGPase), and peroxiredoxin Q plast stroma by in vitro protein import assays (15). We in- (PrxQ) were also bound to TrxL2CS (SI Appendix, Fig. S5B). It vestigated whether TrxL2 is physically associated with the should be noticed that most of these are already known to be thylakoid membrane. Intact chloroplasts were isolated from Trx-targeted proteins that exhibit dynamic redox shifts in re- Arabidopsis leaves and then fractionated into stroma and thyla- sponse to changes in light intensity (12, 13, 19–21). koid membrane. Immunoblotting analyses using antibodies against TrxL2.1 and TrxL2.2 indicated that both TrxL2 isoforms TrxL2 Fails to Reduce FBPase, SBPase, and RCA. The capture of are exclusively localized to chloroplast stroma (SI Appendix, several Trx-targeted proteins by TrxL2CS (described above) Fig. S2). raised the possibility
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