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First published online September 7, 2007; 10.1104/pp.107.105866 Plant Physiology 145:668-679 (2007) © 2007 American Society of Plant Biologists OPEN ACCESS ARTICLE
Distinct Functions for the Two PsbP-Like Proteins PPL1 and PPL2 in the Chloroplast Thylakoid Lumen of Arabidopsis1,[W],[OA]Graduate School of Biostudies, Kyoto University, Sakyo-ku, Kyoto 606–8502, Japan
PsbP, an extrinsic subunit of photosystem II (PSII), is a nuclear-encoded protein that optimizes the water-splitting reaction in vivo. In addition to PsbP, higher plants have two nuclear-encoded genes for PsbP homologs (PsbP-like proteins [PPLs]) that show significant sequence similarity to a cyanobacterial PsbP homolog (cyanoP); however, the function of PPLs in higher plants has not yet been elucidated. In this study, we characterized Arabidopsis (Arabidopsis thaliana) mutants lacking either of two PPLs, PPL1 and PPL2. Phylogenetic analysis suggests that PPL1 would be an ortholog of cyanoP, and PPL2 and PsbP may have a paralogous relationship with PPL1. Analysis on mRNA expression profiles showed that PPL1 expressed under stress conditions and PPL2 coexpressed with the subunits of chloroplast NAD(P)H dehydrogenase (NDH) complex. Consistent with these suggestions, PSII activity in a ppl1 mutant was more sensitive to high-intensity light than wild type, and the recovery of photoinhibited PSII activity was delayed in ppl1 plants. Therefore, PPL1 is required for efficient repair of photodamaged PSII. Furthermore, the stoichiometric level and activity of the chloroplast NDH complex in thylakoids were severely decreased in a ppl2 mutant, demonstrating that PPL2 is a novel thylakoid lumenal factor required for accumulation of the chloroplast NDH complex. These results suggest that during endosymbiosis and subsequent gene transfer to the host nucleus, cyanoP from ancient cyanobacteria evolved into PPL1, PPL2, and PsbP, and each of them has a distinct role in photosynthetic electron transfer in Arabidopsis.
Current evidence suggests that chloroplasts arose more than 1.2 billion years ago (Butterfield, 2000  ) when a free-living cyanobacterium became an endosymbiont in a eukaryotic host. The subsequent evolutionary process of endosymbiotic gene transfer (Brown, 2003), which entailed the transfer of many genes to the eukaryotic host nucleus, dramatically reduced the size of the chloroplast genome. Endosymbiotic gene transfer appears to be a very widespread and continual process (Huang et al., 2005); about 18% of the nuclear genes in Arabidopsis (Arabidopsis thaliana) seem to have come from cyanobacteria, and obvious remnants of chloroplast DNA have been found in higher plant nuclear chromosomes. It is thought that the transfer of genes from the chloroplast genome to the nuclear genome results in greater diversification of gene structure and function; some of these nuclear-encoded genes gained a new function after undergoing internal gene duplication and they are involved in regulation of chloroplast functions (Leister, 2003). For example, the cyanobacterial high-light-inducible protein gene is thought to have evolved into nuclear genes encoding early-light-inducible proteins, stress-enhanced proteins, and light-harvesting complex proteins in higher plants and to have various functions, such as photoprotection or capturing light energy (Montané and Kloppstech, 2000). This diversification of gene function from ancient cyanobacteria enables chloroplasts to adapt their function to the living environment.
The characteristic common to chloroplasts and cyanobacteria is oxygenic photosynthesis, which generates molecular oxygen from the water-splitting reaction. This oxygen-evolving reaction is catalyzed by the protein complex, PSII, composed of intrinsic and extrinsic membrane protein subunits. Interestingly, many intrinsic subunits are still encoded by chloroplast genomes, whereas most extrinsic subunits of eukaryotic oxyphototrophs are nuclear-encoded proteins. This suggests that extrinsic subunits should be susceptible to diversification. In fact, the intrinsic subunits are highly conserved in all known oxygenic photosynthetic organisms, including higher plants, green and nongreen algae, and cyanobacteria, whereas the repertoire of extrinsic subunits that stabilize the function and activity of the oxygen-evolving center differs significantly among those organisms (for review, see Bricker and Burnap, 2005
Recently, genomic and proteomic studies have demonstrated the existence of the PsbP and PsbQ homologs, cyanobacterial PsbP (cyanoP) and PsbQ (cyanoQ), respectively, in cyanobacteria (De Las Rivas et al., 2004 In this study, we characterized two PsbP homologs, PsbP-LIKE PROTEIN1 (PPL1 [At3g55330]) and PPL2 [At2g39470]), in Arabidopsis. To investigate their functions, we characterized mutants lacking PPL1 and PPL2. Analysis of a ppl1 mutant suggested that PPL1 is required for efficient repair of photodamaged PSII under high-intensity light. On the other hand, the stoichiometric level of a subunit of the chloroplast NAD(P)H dehydrogenase (NDH) complex in thylakoid membranes and activity of the complex were severely decreased in a ppl2 mutant, suggesting that PPL2 is a novel thylakoid lumenal factor required for the accumulation of the NDH complex. These results demonstrate the differential functions of PsbP and PPL proteins in the thylakoid lumen of Arabidopsis.
PsbP Protein Family in Arabidopsis
A position-specific iterated-BLAST search of the National Center for Biotechnology Information databases with the sequence of cyanoP (sll1418) hits eight PsbP homologs in addition to two authentic PsbPs (PsbP1 [At1g06680] and PsbP2 [At2g30790]) in Arabidopsis. Based on the amino acid sequence similarity with PsbP1, we classified them into three groups: two PsbP proteins, two PPL proteins, and six PsbP domain (PPD) proteins (Table I
). Two PPL proteins show significantly higher similarity with the PsbP1 sequence (near 40% similarity) than the other six PPD proteins, and a BLASTP search of The Arabidopsis Information Resource database (http://www.arabidopsis.org) with the PsbP1 sequence also suggests a close relationship with PsbP1 (PPL1 [At3g55330], E value 9 x 10–6; PPL2 [At2g39470], E value 5 x 10–4). All PsbP homologs in Arabidopsis, except for PPD2, are found in the rice (Oryza sativa) EST database (http://www.ncbi.nlm.nih.gov/dbEST), suggesting that they are conserved in both dicot and monocot plants (Supplemental Fig. S1). All PsbP homologs have an obvious thylakoid lumen-targeting signal, consistent with previous proteomic studies, which has proven their localization in the thylakoid lumen, except for PsbP2 (Peltier et al., 2002
Two PPL Proteins, PPL1 and PPL2, Are Well Conserved among Higher Plants Searching genome or EST databases by the tBLASTN program identified orthologs of PPL1 and PPL2 in all plant species we checked with highly conserved amino acid sequences (Supplemental Fig. S2). Chlamydomonas reinhardtii, which contains PsbP, has no PPL protein orthologs, whereas Chlamydomonas incerta has a PPL1 homolog in spite of PsbP proteins. Cyanidioschyzon merolae has two PPL proteins, whose sequences are closer to cyanoP than to PPL proteins in higher plants. These results suggest that both PPL1 and PPL2 would be well-conserved proteins in higher plants, but not in chlorophytes or rhodophytes. Based on the alignment of cyanoP, PPL, and PsbP sequences, a phylogenetic tree was constructed (Fig. 1A ). As expected, cyanoP and PPL sequences branched into a different clade from PsbP sequences. Alignment of the amino acid sequences suggests that both PPL1 and PPL2 are much more similar to cyanoP than to PsbP in higher plants (Fig. 2 ). In particular, PPL1 is more similar to cyanoP than PPL2 and also contains a His residue conserved in all cyanoPs and PsbPs (Fig. 2, asterisk). These facts suggest that PPL1 is closely related to cyanoP, whereas PsbP and PPL2 may have a paralogous relationship with PPL1. High conservation of PsbP and PPLs indicates their important function in higher plants.
mRNA Expression Profiles Differ Significantly between the Two PPLs
To estimate functions of PPL1 or PPL2, we searched for genes that are coexpressed with these genes using a program in ATTED-II using Pearson's correlation coefficient (r) for neighboring pairs of genes (see "Materials and Methods"). Nine genes were found to be coexpressed with PPL1 with a high r value (r
In the case of PPL2, six genes were coexpressed with PPL2 with a high r value (r The above results indicate that both PPL1 and PPL2 would have a function related to photosynthesis, presumably under certain stress conditions, such as high-intensity light. However, based on microarray data, the spectrum of genes coexpressed with PPL1 is significantly different from that coexpressed with PPL2, suggesting that the function of PPL1 and PPL2 genes differs in Arabidopsis.
To elucidate the functions of PPL1 and PPL2 proteins, we used a ppl1 mutant (salk_014843) containing a single T-DNA insertion located in intron 4 and a ppl2 mutant (salk_020674) containing two T-DNA insertions located in exon 5 (Supplemental Fig. S3A). The PPL1 or PPL2 mRNA was undetectable by reverse transcription (RT)-PCR in the respective mutants (Supplemental Fig. S3B), indicating that the T-DNA insertions had disrupted expression. Under normal growth conditions (10/14-h photoperiod at 100–200 µmol quanta m–2 s–1, 21°C), both ppl1 and ppl2 plants showed nearly wild-type growth (Supplemental Fig. S3C).
The parameters for the photosynthetic properties showed that the maximal quantum yield of PSII (Fv/Fm), the relative amount of far-red oxidizable P700, and the chl a/b ratio were not significantly different between mutants and wild-type plants (Table II
). Therefore, the steady-state properties of PSII and PSI in dark-adapted leaves were not affected in both ppl1 and ppl2 plants. However, under actinic light (AL) illumination (144 µmol photons m–2 s–1), ppl2 plants showed significantly lower
The oxygen-evolving activities of isolated thylakoid membranes were then examined on the chl basis with p-phenylbenzoquinone as an electron acceptor (Table II). The maximal activity from ppl1 thylakoids was significantly lower than those from wild-type and ppl2, and a similar observation was obtained in the further presence of 2,5-dibromo-6-isopropyl-3-methyl-1,4-benzoquinonine, which blocks the electron transfer between PSII and PSI (data not shown). Because the ratio of the average activity during first 5 min to the maximal (initial) activity after light illumination was almost the same among the samples (approximately 70%), the stability of active PSII was not significantly different, which was consistent with the normal value of Fv/Fm in ppl1 mutants.
To investigate whether a deficiency of PPL1 or PPL2 affects the normal accumulation of thylakoid membrane proteins, immunoblot analysis was conducted on isolated thylakoid membranes of ppl1 and ppl2 mutants. In addition to the protein subunits of the major protein complexes, such as PSII and PSI located in thylakoids, a protein blot was also probed with antibodies against the NdhH subunit of the NDH complex because our bioinformatics analysis suggested that PPL2 was coexpressed with the subunits of the chloroplastic NDH complex (Fig. 1C; Supplemental Table S2). Previous study showed that the NdhH subunit is unstable without other NDH subunits (Munekage et al., 2004
Despite the lower activity of oxygen evolution, deletion of PPL1 did not substantially affect the accumulation of thylakoid membrane proteins (Fig. 3
). On the other hand, interestingly, the amount of NdhH was markedly reduced in the ppl2 mutant (
Arabidopsis ppl1 Mutant Was Sensitive to High-Intensity Light-Induced PSII Photoinhibition The bioinformatics analysis shows that PPL1 is coexpressed with TLP40 and SEP1, suggesting that its expression is induced in response to stress (Fig. 1B; Supplemental Table S1). Then, we examined the performance of PSII in wild type, ppl1, and ppl1 + PPL1 plants under high-intensity light. Detached leaves were irradiated with high-intensity light, and Fv/Fm was monitored. Under high-intensity light (550 µmol photons m–2 s–1), wild-type leaves showed little decline in Fv/Fm (Fig. 4A ). However, in the ppl1 mutant, Fv/Fm decreased to about 70% of the initial value within 200 min of illumination, clearly showing increased photoinhibition in the ppl1 mutant compared to wild-type plants. In the presence of chloramphenicol, which inhibits plastid protein synthesis, Fv/Fm decreased to about 60% within 200 min of illumination in both ppl1 and wild-type leaves. Increased photoinhibition in ppl1 leaves compared to wild-type leaves was also observed under further higher intensity light (1,200 µmol photons m–2 s–1; Fig. 4B). In addition, the photobleaching phenotype was observed in the ppl1 leaves after high-intensity light treatment (data not shown). These results demonstrate that ppl1 leaves are more sensitive to high-intensity light-induced photoinhibition than wild-type leaves, whereas wild-type and ppl1 leaves have potentially similar rates of PSII photodamage.
To examine whether high-intensity light-induced PSII inactivation led to a decrease in the steady-state level of PSII complexes, we analyzed the accumulation of D1 proteins in leaves from ppl1 mutants and wild-type plants under high-intensity light. As shown in Figure 4, the amount of D1 proteins declined gradually in leaves from ppl1 mutants and wild-type plants, and the extent of the decrease was much larger in the ppl1 mutant (Fig. 4C). In the presence of chloramphenicol, the amount of D1 proteins declined rapidly in both ppl1 mutants and wild-type plants and no apparent difference was observed. These phenotypes in the ppl1 mutant were fully recoverable in ppl1 + PPL1 leaves.
To investigate further the reason for high sensitivity of ppl1 leaves to high light illumination, the capability for recovery from photoinhibition and the susceptibility to photodamage were separately compared in wild-type and ppl1 leaves under moderate light conditions. To analyze the recovery process, light intensity was lowered until 150 µmol photons m–2 s–1 after photoinhibitory treatment and recovery of the Fv/Fm values were monitored. As shown in Figure 5A , recovery of Fv/Fm values in ppl1 leaves was significantly slower than that in wild-type leaves: Fv/Fm values in the ppl1 leaves was still approximately 90% of the initial Fv/Fm values even after the 24-h recovery period. On the other hand, no noticeable difference of PSII damage was observed between wild-type and ppl1 leaves at this condition as observed under higher illumination (Figs. 4, A and B, and 5B). These results suggest that PPL1 is required for efficient repair of photodamaged PSII.
Arabidopsis ppl2 Mutant Is Defective in NDH Activity in Vivo
Because the immunoblot analysis suggested the absence of NDH complexes in ppl2 mutants, NDH activity of these plants was examined. The NDH complex catalyzes electron donation to PQ from the stromal electron pool (Fig. 6A
). The activity of NDH can be monitored as a transient increase in chl fluorescence after turning off AL illumination (Fig. 6B; Burrows et al., 1998
PPL1 Proteins Are Not Tightly Associated with PSII
Our results described above suggested that PPL1 had a function in PSII, although its function was different from that of PsbP. We then examined whether PPL1 was associated with PSII by blue native (BN)-PAGE. Thylakoid membranes isolated from wild-type plants were solubilized with n-dodecyl-
In this study, we demonstrate that two PPL proteins, PPL1 and PPL2, have distinct functions in the thylakoids in Arabidopsis: PPL1 is required for the efficient repair of photodamaged PSII and PPL2 is crucial for the accumulation of the chloroplastic NDH complex. PPL proteins are highly conserved among higher plants, suggesting their general importance in plant photosynthesis.
Phylogenic analysis suggests that the PPL1 protein is a putative ortholog of cyanoP in higher plants (Fig. 1A). Knockout of PPL1 in Arabidopsis made the plant sensitive to high-intensity light (Fig. 4). This change was similar to, but much milder than, the effects observed in PsbP-RNAi plants (Ifuku et al., 2005
Recently, it has been reported that another lumenal protein, Psb27, is also required for efficient repair of photodamaged PSII in Arabidopsis (Chen et al., 2006
Although PsbP, PPL1, and cyanoP seem to be functionally related, PPL2 has quite a different role related to the chloroplastic NDH complex. Whereas many subunits of the chloroplastic NDH complex are similar to those of the prokaryotic respiratory complex-I (NDH-I), the chloroplastic NDH complex has extra subunits that are unique to cyanobacteria and higher plants. Recently, a biochemical and genetic approach identified many candidate NDH subunits (Munshi et al., 2005
We have demonstrated divergent and important functions of PPL proteins in higher plants. PsbP is a representative of the PsbP protein family (Pfam [PF01789]), and the protein folding of PsbP is classified in the Mog1p/PsbP-like superfamily in the Structural Classification of Proteins database (http://scop.mrc-lmb.cam.ac.uk/scop). In addition to PsbP and two PPL proteins, Arabidopsis has six PPD proteins, although nothing is known about their physiological functions (Table I). Despite the high-resolution structure of PsbP (Ifuku et al., 2004 ), the molecular mechanism of PsbP function (i.e. the binding mode to PSII and the manner of ion retention) has not been elucidated, and thus the importance of PsbP domain remains unclear. Further studies on the molecular function of PsbP, PPL, and other PPD proteins should reveal the nature of this diverged protein family and such information will be important for studies of the evolution of oxygenic photosynthetic organisms.
Bioinformatics Analysis
PsbP homologs were searched for nonredundant protein sequence databases in Arabidopsis (Arabidopsis thaliana) by the position-specific iterated-BLAST program (http://www.ncbi.nlm.nih.gov) using cyanoP as a query (GenBank accession no. P73952). Amino acid sequences of PsbP family proteins were aligned by the ClustalW program and the percentage of amino acid sequence identity (similarity) was calculated for the regions corresponding to Met-1-Tyr-188 or Ala-78-Ala-263 of cyanoP or Arabidopsis PsbP1, respectively. PPL homologs (E value of the best match
To search for genes coexpressed with PPL1 or PPL2, we used Pearson's correlation coefficient (r) for each pair of genes, which was calculated using the 771 Affymetrix ATH1 array data from AtGenExpress (Schmid et al., 2005
Arabidopsis wild-type (ecotype Columbia-0 [Col-0]), ppl1, ppl2, and crr2 were grown in soil under growth chamber conditions (10/14-h photoperiod at 100–200 µmol photons m–2 s–1, 21°C) for 3 to 4 weeks. Seeds for the T-DNA insertional mutants of PPL1 (At3g55330) and PPL2 (At2g39470) were purchased from a collection developed at the Salk Institute Genomic Analysis Laboratory (Alonso et al., 2003
The following primer sets were used to amplify PPL1 and PPL2 cDNA: PPL1 (Fw 5'-CACCATGGCTTCTCTGAAGCTTTCAC-3' and Rv 5'-TCAAACAGTGATCTTGAAGGAATCT-3') and PPL2 (Fw 5'-CACCATGGCAGTCTCCTCACTCTCA-3' and Rv 5'-TCAAATCTGAAGGATCTTCAAAGAGT-3'). The PCR products were cloned into the pENTR TOPO vector (Invitrogen) and transferred from the entry constructs into the pGWB2 vector by a LR recombination reaction (Gateway; Invitrogen). The plasmids pGWB2-PPL1 and pGWB2-PPL2, in which the expression of each cDNA is driven by the 35S promoter, were used to transform homozygous ppl1 and ppl2 mutants via Agrobacterium tumefaciens strain GV3101 (Clough and Bent, 1998
Chl fluorescence was measured with a PAM2000 (pulse-amplitude modulation) chl fluorometer (Walz). Minimal fluorescence at open PSII centers in the dark-adapted state (F0) was excited by a weak measuring light (650 nm) at a light intensity of 0.05 to 0.1 µmol photons m–2 s–1. A saturating pulse of white light (800 ms, 3,000 µmol photons m–2 s–1) was applied to determine the maximal fluorescence at closed PSII centers in the dark-adapted state (Fm) and during AL illumination (Fm'). The quantum yield of PSII ( The change in the absorbance of P700 at 810 nm was measured with a PAM101 chl fluorometer with an ED-P700DW-E emitter-detector unit (Walz). The change in absorbance induced by saturating far-red light represents the relative amount of photooxidizable P700.
Oxygen evolution from thylakoid membranes was measured at 25°C with a Clark-type oxygen electrode (Hanzatech) under saturating red light with an R-60 red long-pass filter (Kenko). The buffer for measurement was 50 mM HEPES-NaOH, pH 7.6, containing 0.4 M Suc, 10 mM NaCl, 5 mM MgCl2, with an uncoupler (5 mM NH4Cl) and an electron acceptor for PSII (0.5 mM p-phenylbenzoquinone).
To isolate thylakoid membranes, leaves were chopped in a blender with ice-cold buffer (50 mM HEPES-NaOH, pH 7.6, containing 0.4 M Suc, 10 mM NaCl, 5 mM MgCl2, and 5 mM sodium ascorbate). The mixture was then filtered and centrifuged and the pellet was washed and resuspended in the same buffer without the sodium ascorbate. The chl content of thylakoid membranes was determined as described in Arnon and Whatley (1949)
The nucleotide sequences encoding the amino acid residues from 75 to 230 of PPL1 and from 84 to 240 of PPL2 were amplified by RT-PCR using the following primer sets: PPL1 (5'-CATATGGCAGAAAGCAAAAAAGGATTC-3' and 5'-CTCGAGAACAGTGATCTTGAAGGAATCTAC-3') and PPL2 (5'-CATATGGAAGAGATACCAAAAAGCTACTCG-3' and 5'-CTCGAGAATCTGAAGGATCTTCAAAGAGTC-3'). Amplified cDNAs were inserted in frame into the expression vector pET22b (Novagen) such that the His tag was fused at the C-terminal end. The resulting plasmids of PPL1 and PPL2 were transformed into Escherichia coli strain Rosettagami (DE3; Novagen) or BL21 (DE3), respectively. Expression of the PPL1-His or PPL2-His fusion protein was induced by adding 1 mM isopropyl
Rabbit antibodies against spinach (Spinacia oleracea) PsbP, Arabidopsis PPL1, Arabidopsis PPL2, and tobacco (Nicotiana tabacum) NdhH were produced by the authors. Rabbit antibodies against D1 peptides were produced by Dr. Y. Yamamoto (Okayama University). Rabbit antibodies against spinach PsbO and PsbQ were provided by the late Dr. A. Watanabe (Tokyo University). Rabbit antibody against Chlamydomonas PsaA/B (CP1) was provided by Dr. A. Tanaka (Hokkaido University). Rabbit antibody against spinach CP43 was a gift from Dr. Y. Kashino (Hyogo Prefectural University).
Detached leaves, placing adaxial side up on the filter papers steeped with a sodium phosphate buffer (NaOH/pH7.0), were illuminated at 550 or 1,200 µmol photons m–2 s–1. To examine the role of chloroplast-encoded protein synthesis in the susceptibility of leaves to photoinhibition, detached leaves were incubated with the buffer including 200 µg mL–1 chloramphenicol under reduced pressure for 5 min prior to photoinhibitory light treatment. To analyze the accumulation of D1 proteins under high-intensity light, proteins were extracted from leaves ground in liquid nitrogen and used for SDS-PAGE and subsequent immunoblotting against D1 antibodies.
Saturating white light (3 min, 3,000 µmol photons m–2 s–1) was illuminated five to eight times at 3-min intervals on detached leaves and resulted in about 50% of the initial Fv/Fm values in wild-type and ppl1 leaves. Following that, the changes in Fv/Fm values from wild-type and ppl1 leaves were seen during the recovery period at irradiance of 150 µmol photons m–2 s–1, 30°C.
BN-PAGE was performed as described (Schägger et al., 1994 Sequence data from this article can be found in the GenBank/EMBL data libraries under accession numbers NM_115391 (PPL1) and NM_129505 (PPL2).
The following materials are available in the online version of this article.
We thank all of the investigators who kindly provided specific antibodies as listed in "Materials and Methods." We also thank Dr. T. Nakagawa (Research Institute for Molecular Genetics, Shimane University), who kindly provided us with pGWB2 vectors, and Dr. T. Shikanai (Kyushu University), who kindly provided us with the crr2 mutant. Received July 22, 2007; accepted September 4, 2007; published September 7, 2007.
1 This work was supported by a Grant-in-Aid from the Ministry of Education, Culture, Sports, Science and Technology, Japan, for Scientific Research on Priority Areas (grant no. 17051016 to K.I. and F.S.) and for Young Scientists (B; grant no. 18770032 to K.I.), and a Research Grant from Nissan Science Foundation (to K.I.).  The authors responsible for distribution of materials integral to the findings presented in this article in accordance with the policy described in the Instructions for Authors (www.plantphysiol.org) is: Kentaro Ifuku (ifuku{at}kais.kyoto-u.ac.jp).
[W] The online version of this article contains Web-only data.
[OA] Open Access articles can be viewed online without a subscription. www.plantphysiol.org/cgi/doi/10.1104/pp.107.105866 * Corresponding author; e-mail ifuku{at}kais.kyoto-u.ac.jp.
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ABSTRACT
RESULTS
0.925; thin black lines, 0.925 > r 
PSII values (0.613 ± 0.015) and ppl1 plants showed slightly lower 
12.5% of wild-type NdhH levels) and comparable to that seen for the NDH mutant crr2 (chlororespiratory reduction2), which lacks the pentatrico peptide repeat protein needed for the intergenic RNA processing essential for the translation of NdhB (Hashimoto et al., 2003
-D-maltoside, and the protein complexes were separated in a BN gel. After BN-PAGE, the separated protein complexes were blotted on the membrane and further subjected to immunoblot analysis using specific antibodies against PPL1 and PPL2 (Supplemental Fig. S4). The immunoblots using anti D1 and CP43 antibodies showed signal bands from PSII supercomplexes, dimeric PSII, monomeric PSII, and CP43-less PSII at the positions of approximately 669, 440, 240, and 200 kD, respectively (
