1. Introduction
Photosystem I (PSI) from cyanobacteria and chloroplasts is a multisubunit membrane-protein complex that catalyses electron transfer from reduced plastocyanin in the thylakoid lumen to oxidized ferredoxin in the chloroplast stroma or cyanobacterial cytoplasm [1-4]. PSI is responsible for NADP+ reduction and cyclic photophosphorylation and consists of at least 8 polypeptides. Its major components are the P700 chlorophyll a A1 and A2 apoproteins whose molecular weights vary between 60 and 70 kd, depending on the species [5]. In this chapter, we discuss recent progress on several topics related to the functions of the PSI complex, like the protein composition of the complex in the plant and algae, the structure and organization of the PSI subunits and the regulation of photosystem I-related gene under abiotic stress conditions. Furthermore, PSI seems to be well protected from photoinhibition in vivo in many plant and algae species and many environmental conditions. The physiology and molecular mechanism during short term adaptation to changes under oxidative stress is discussed in functional and structural terms. Finally, such characteristics of PSI photoinhibition with special emphasis on the relationship between two photosystems as well as the protective mechanism of PSI in vivo is reviewed with respect to function of the thylakoid membrane.
2. Structure of photosystem I
PSI catalyzes the light-driven electron transfer from the soluble electron carrier plastocyanin on the luminal side of thylakoid membrane, to ferredoxin on the stromal side of thylakoid membrane. In plants, the PSI complex consists of at least 19 protein subunits, approximately 175 chlorophyll molecules, 2 phylloquinones and 3 Fe4S4 clusters [6]. The crystal structure of PSI from
The PSI complex of most plants and algae consists of 13 subunits: at least five chloroplast-encoded subunits (PsaA, PsaB, PsaC, PsaI and PsaJ) and eight nucleusencoded subunits (PsaD, PsaE, PsaF, PsaG, PsaH, PsaK, PsaL, PsaN) and numerous redox cofactors and antenna chlorophylls [8]. An additional subunit, PsaM, has only been found in cyanobacteria and in the chloroplast genomes of some lower plants and algae. The PSI subunits PsaG, PsaH and PsaN are only found in eukaryotic photosynthetic organisms and are missing in cyanobacteria[8,9,10].
2.1. Subunits of PSI
2.1.1. PsaA and PsaB
The major subunits of photosystem I,
Previous studies showed that mutants deficient in PsaB are unable to synthesize both PsaB and PsaA whereas mutants affected primarily in PsaA synthesis are still able to produce PsaB [2,3,11]. Based on these results it was proposed that PsaB is an anchor protein during PSI assembly, which needs to be synthesized and integrated into the thylakoid membrane before the other PSI subunits are synthesized [12]. In its absence these polypeptides are no longer synthesized and/or are rapidly degraded. Elucidating how PsaB is translated and inserted into the thylakoid membrane is thus important for understanding the initial steps of PSI assembly.
2.1.2. PsaC, PsaD and PsaE
The subunits PsaC, PsaD and PsaE do not contain transmembrane α-helices [3,2,14]. They are located on the stromal side of the complex, forming the stromal hump. They are in close contact to the stromal loop regions of PsaA and PsaB. Subunit PsaC carries the two terminal FeS clusters FA and FB, and is located in the central part of the stromal hump. PsaD forms the part of this hump, which is closest to the trimeric axis [15,2,3]. The C-terminal part of PsaD forms a `clamp' surrounding PsaC. PsaE is located on the side of the hump, which is distal from the trimer axis[16,17].
The clusters of PsaC are characterised by their distinct electron paramagnetic resonance (EPR) spectra [18,19]. PsaC is likely to posses a pseudo-C2 symmetry axis that is oriented perpendicular to distance vector connecting the two iron-sulfur clusters, FA and FB. The role of subunit PsaC in coordination of the two terminal FeS clusters was suggested from the conserved sequence motif CXXCXXCXXXCP which is found twice in the gene of PsaC [3,20]. A homology of subunit PsaC to bacterial ferredoxins, also containing two [4Fe-4S] clusters, was proposed from sequence similarity [21]. The structures of PsaC and these ferredoxins, such as that from
PsaD is a peripheral subunit of photosystem I (PSI1), an integral protein complex in the thylakoid membrane of oxygenic photosynthetic organisms. Biochemical experiments [20, 21] and analyses of the primary structure of PsaD suggest that it does not posses a transmembranal segment and that it faces the stromal side of the thylakoid membrane. The PsaD is a polypeptide of 139-144 amino acids in cyanobacteria, but has an N-terminal extension of several residues in higher plants, yielding a total length of 158-162 residues [20]. Topological studies [3, 2, 19, 22, 23] and data from an X-ray structure of PSI at 4 Å [24, 25]show that PsaD probably contains an R-helix and is in contact principally with PsaC and PsaE, and also with PsaH and PsaL [25, 26, 27]. The three-dimensional structure of the higher-plant PSI as determined by electron crystallography has been recently reported [27], confirming that the stromal ridge of higher-plant PSI can also be interpreted as being due to the PsaC, -D, and -E subunits. The N-terminal part of the PsaD subunit can be accessed by the proteases, and its C-terminal region is exposed to solvent [23, 14]. Comparison of the amino acid sequences of PsaD from several species shows that the C-terminal part is highly conserved, especially in a region containing many basic residues[23].
In spinach, PsaD is synthesized in the cytoplasm as a precursor of 23.2 kDa [2,23, 21] that is processed to produce the mature 17.9-kDa PasD. In vitro assembly assays indicated that both forms of the protein, pre-PsaD and PsaD, can assemble into the thylakoid membranes, specifically into the PSI complex [2, 14, 22, 24, 25, 26]
PsaD is known to interact strongly with ferredoxin. Chemical cross-linking of PSI and ferredoxin consistently yield a product consisting of PSI-D and ferredoxin [14, 23, 25], and recently the interaction has been shown even with isolated PSI-D and ferredoxin [47]. These observations clearly point to an important function of PSI-D in docking of ferredoxin in both eukaryotes and cyanobacteria. The position of ferredoxin in these crosslinked complexes was also identified by electron microscopy [28]. The same docking site was also found for flavodoxin [29] and is in agreement with a docking site proposed from the structural model of PS I at 6 Å resolution. Subunit PsaD is essential for electron transfer to ferredoxin [28].
PsaE is like PsaD a hydrophilic subunit exposed to the stroma. PsaE is encoded in the nucleus and the mature protein is about 11 kDa. Just like PsaD, the mature PsaE in plants has an extended N-terminal region. The extension is variable from 30-40 amino acid residues. As was the case for PsaD, there is no extension in the chloroplast encoded PsaE in
The structure of subunit PsaE (8 kDa) in solution was determined by 1H and 15N-NMR [32, 33]. The loop connecting L-strands 3 and 4 was found to be flexible in the NMR structure[33]. The structure of PsaE in the PSI complex is very similar to the solution structure, with some remarkable deviations in the loop region E-L3L4, which corresponds to the CD loop in the NMR structure. The twist of this loop reported at 4 Å [34] is fully confirmed in the structural model at 2.5 Å resolution. This loop is involved in interactions with PsaA, PsaB and PsaC, suggesting a change of the loop conformation during assembly of the photosystem I complex.
Different functions have been reported for PsaE. PsaE in barley has also been found to be associated with ferredoxin NADP oxidoreductase (FNR) [35]. In cyanobacteria, FNR has a domain linking it to the phycobilisomes [36]. However, recent observations have shown that in spite of this domain, FNR does appear to interact with PsaE [37].
2.1.3. Other subunits of PSI
Six small intrinsic membrane protein components of photosystem I have been identified from the gene sequence in
The small subunits can also be divided into two groups according to their location in the complex: PsaL, PsaI and PsaM are located in the region where the adjacent monomers face each other in the trimeric PS I complex, whereas PsaF, PsaJ, PsaK and PsaX are located at the detergent exposed surface of photosystem[40].
PsaF binds the luminal electron donor, plastocyanin [41, 42, 43, 44], and It is essential for providing excitation energy transfer from LHCI to the core complex. Early work showed that PsaF (then called subunit III) was required for electron transfer from Pc to P700 [45, 46]. Subsequently, it was demonstrated that Pc cross-linked to PSI is capable of fast electron transfer to P700 and the cross-linking partner was identified as PsaF.
PsaG and PsaK are two small membrane intrinsic proteins of approximately 10-11 kDa each with two transmembrane α-helices connected by a stromal-exposed loop [47, 48] and they show a 30 % sequence homology in
PsaH is a 10 kDa protein with one predicted transmembrane helix [54]. The subunit can be chemically cross-linked to PsaD, PsaI and PsaL [50, 54, 55, 56]. Thus, PsaH must be located near the region that constitutes the domain of interaction between monomers in
PsaN is a small extrinsic subunit of about 10 kDa [54]. PsaN is synthesized with a presequence directing it to the lumen and is the only subunit located exclusively on the lumenal side of PSI [59]. The Psa-G, -H, and -N fulfill functions in PSI that are unique to eukaryotic PSI. PsaH has been shown to be involved in state 1–state 2 transitions probably in the interaction with LHCII [54], PsaN is involved in interaction with plastocyanin [41], and PsaG is involved in the stabilization of LHCI and regulation of PSI activity [53]. It is therefore likely that PsaO plays a role in the interaction between the PSI core and other complexes in the thylakoid membrane such as LHCI or LHCII [50, 60]. Alternatively PsaO is involved in the regulation or fine tuning of PSI activity. Together with PsaO, the subunits Psa-G, -H, and -N are unique to higher plants and algae. Structure of plant PSI at 4.4 Å, the structure and position of the Psa-G and -H subunits within the PSI complex are revealed [49]. However, Psa-N and -O are either not resolved at the current resolution or are lost from the complex during preparation and their structure and exact position in the PSI complex are therefore not known.
PsaJ is a hydrophobic subunit of 4-5 kDa. The protein is chloroplast encoded as is the case also for PsaI, which has a similar size and hydrophobicity [54]. PsaJ is located near PsaF as evidenced by cross-linking [56]. The protein has been thought to be membrane spanning, however, the structural model of cyanobacterial PSI suggest that PsaJ may form an unusual bend helix in the plane of the membrane [60]. In the unicellular green alga
Psa-K from spinach may be tightly associated with the PSIA/B heterodimer [61, 62]. However, PsaK from spinach, pea, and barley was depleted from the PSI core by methods used for separation of LHCI from PSI [65, 64]. Treatment of thylakoids with proteases resulted in degradation of PsaK, indicating that part of the PSI-K polypeptide is exposed on the stromal side of the thylakoid membrane. It has therefore been proposed that the membrane-spanning PsaK subunit is located near the rim of the PSI complex between the PSI and LHCI and is thus easily lost upon detergent treatment [51].
There is significant sequence similarity between PsaG and PsaK from eukaryotes [64]. A computer comparison of PsaG and PsaK from
2.2. Light harvesting complex I
X-ray crystallography of the PSI core from cyanobacteria [22, 25, 50, 55] as well as modeling studies indicates strong interpigment interactions and unique protein environment as a source for the low energy shifts in absorption of PSI. Biochemical and spectroscopic studies of Light Harvesting Complex I (LHCI) suggest that in the PSI-LHCI super complexes the peripheral antenna and the PSI core antenna have structurally and spectrally distinct pools of red pigments [22]. As in the PSI core antenna, excitonically coupled dimers or trimers of Chl
3. Photosytem I antenna
3.1. Core antenna
The antenna of PSI consists of two structurally and functionally parts; the core antenna and preripheral antenna.
The core antenna of PSI contains in total appromeximately 100 chla and 15 β-carotene of which the majority is bound to the PsaA/PsaB dimmer [49]. The chlorophylls have their Q4 absorption maxima around 680 nm. A comparison of absorbtion spectra of PSI, LHCI complexes from wild type A, thaliana and from a mutant lacking the PsaL and PsaH subunits revealed that the about five chlorophylls that are bound to these subunits absorb preferentially at 638 and 667 nm [73].
3.2. Prephral antenna
The prepheral antenna of PSI consists of nuclear encoded chlorophyll binding proteins (Lhca) which are transported into the chloroplast and form a light-harvesting complex (LHCI) which increases the light-harvesting capacity of PSI [74].
The protein contacts between the core complex and LHCI appear to be relatively weak, which explains the biochemical sensitivity of the PSI-LHCI supercomplex to detergent attack. It is clear, however, that each of the four light-harvesting proteins fits its specific binding site, because the interface of the core complex formed by subunits PsaG, PsaB, PsaF, PsaJ, PsaA, and PsaK is asymmetric [4, 49]. Lhca1 antenna protein is bound to the core through PsaB and PsaG. Previous studies showed that plants in which
4. Role of the PSI subunits specific to plants and algae
The extrinsic protein, PsaD, has two reported functions in the PS I complex of cyanobacteria, algae and higher plants. The first function, deduced from
While the function of the ten PSI subunits common to plants, algae and cyanobacteria has been studied extensively, the role of the three eukaryotic-specific subunits PsaH, PsaG and PsaN is less well understood. One reason is that these subunits are nucleus-encoded and thus less amenable to genetic manipulation [2, 53]. However it has recently been possible to generate transgenic
The analysis of the PsaF-deficient strain and its suppressor reveals that in the presence of a functional antenna, an intact donor side of PSI is required for protection of
The function of the PsaF protein (15 kDa) at the lumenal side has been subject to discussion. In intact cells of the green alga Chlamydomonas reinhardtii, PsaF is implicated in the electron transfer from plastocyanin to oxidized P700 by providing a docking site for the electron donor: psaFÿ mutants of this organism had a dramatically reduced electron transfer rate [15, 45, 76]. In contrast, a psaFÿ mutant of the cyanobacterium Synechocystis PCC 6803 exhibited normal electron transfer to P700., implying that PsaF is not essential for the docking of either cytochrome c6 or plastocyanin to PSI [15, 76, 82]. While PSI is extracted as a mixture of trimers and monomers from thylakoid membranes of wild-type cyanobacteria, PSI from mutants that lack the PsaL protein (16 kDa) exists exclusively as a monomer after membrane solubilization [73]. In addition, proteolysis studies have shown PsaL to be located about the 3-fold axis of the trimer, thus holding it together [5, 15]. Little is known about the function of the four other membrane intrinsic subunits (PsaI, -J, -K and -M) that have molecular masses ranging from 3 to 8 kDa [63].
Comparison of deduced primary sequences indicates that the PsaL subunits contain a greater diversity than seen in other subunits [15, 54]. Function of PsaL in the formation of PS I trimers was revealed by the inactivation of the psaL gene in
5. Gene of photosystem I
Photosystem I (PSI) is a multiprotein complex in the thylakoid membrane of chloroplasts, providing an interesting system for studying the nucleo-choloroplast relationship in plants.. The core subunits of the PSI reaction centre are still encoded by the chloroplast genome, whereas the genes for the peripheral subunits are located in the nucleus in green algae and land plants. In this study, we dissected the promoter architecture of a nuclear-encoded PSI gene in tobacco, and investigated whether the characteristics found in this promoter are shared by those of the other photosynthesis nuclear genes.
Sequencing of these proteins and/or their corresponding genes have registered two genes,
The genes for the two subunits, psaA and psaB, are located adjacent to each other in the large single-copy region of circular plastid genome in higher plants [89]. Gene psaB is followed by rps14 encoding the chloroplast ribosomal protein CS14 [90]. The psaA-psaB-rps14 gene cluster was found to co-transcribe into a 5- to 6-kb polycistronic mRNA in spinach [91], tobacco [90], and rice [89]. Cheng et. al. [90] have performed a detailed transcriptional analysis of the promoter of rice psaA-psaB-rps14 operon with deleted mutants in vitro. They showed that two functional promoters denoted as “-175” and “-129” were revealed.
Some of the known signals which are targeted to these genes are light, plastid signal(s) and hormones. Nuclear encoded genes of PSI are effectively activated by white and red light, while blue light is less effective. Essential promoter units which are responsive to light were identified by deletions and mutational analyses. Another set of signals is produced by the plastids reporting the state of the plastids to the nucleus. When plastids were bleached by the addition of norflurazon, transcription of nuclear PSI genes was decreased [92]. The nature of these plastid-derived signals has still to be elucidated, however it appears that the communication between the two organelles is mediated by more than one signal [93, 94]. The responsive units within the promoter appear to be the same as the light-responsive elements [93]. The third group of signals acting on genes for thylakoid proteins is plant hormones. Kusnetsov et al. [95] suggested that it could be shown that cytokinin stimulated the transcription of
In the spinach
In higher plants, the function of the nuclear-encoded subunits has been elucidated in recent years using RNAi (RNA interference), antisense techniques and insertional mutagenesis in
6. Photoinhibition of PSI and response to abiotic stress
Plant chloroplasts include two large pigment-protein complexes, such as photosystem I and photosystem II that are located within thylakoid membranes. The reaction centres of PSI and PSII are formed by chlorophyll a-binding heterodimers, PsaA/PsaB and PsbA/PsbD proteins, respectively. PSI and PSII are both organized into supercomplexes with variable amounts of nuclear-encoded chlorophyll a/b-binding proteins forming light-harvesting antenna complexes around PSI (LHCI) and PSII (LHCII) (Figure 1).
Environmental factors such as temperature, UV-light, irradiance, drought and salinity are known to affect photosynthesis in both cyanobacteria and plants (Figure 1). In cyanobacteria, several studies have been reported on photosynthetic electron transport activities both under salt and high light stress conditions in whole cells as well as thylakoid membranes[102,103].
Photoinhibition of Photosystem I (PSI) was first reported by Jones and Kok [104], is the one who originally called them ‘photoinhibition’ [105]. The subsequent studies revealed that the activity of PSI could be photoinhibited in thylakoid membranes [106, 107] as well as in isolated PSI complexes [108, 109]. However, PSI-specific photoinhibition was never observed in intact leaves until 1994 [110]. The selective photoinhibition of PSI was first observed in cucumber leaves treated at chilling temperatures [111]. In contrast PSI is generally believed to be less sensitive to light stress and its photoprotection mechanisms were less investigated. Nevertheless, several recent evidences showed that PSI can also be targeted by photoinhibition, especially under chilling conditions and when the linear electron transport chain is unbalanced [111, 112]. PSI photoprotection has been suggested to be mainly mediated by oxygen scavenging enzymes (e.g., superoxide dismutase and ascorbate peroxidase) which efficiently detoxify reactive species produced at the reducing side of Photosystem I [113]. A decreased ability of these enzymes to scavenge ROS at low temperatures was proposed to be the reason of the major PSI photo-sensitivity in chilling conditions [111, 112, 114]. As a summary, processes during of PSI photoinhibition as follow;
Decreased rate of reducing power utilization by Calvin cycle enzymes (Rubisco) at low temperature;
Photoinduced electron transfer from PS2 and reduction of PS1 electron acceptors (FeS centres, Fd, NADP);
Cold-induced diminish of oxidative defense system (tAPX, sAPX etc.) capacity;
Recombination of separated charges in PS1 reaction centres between P700+ and A0 – or A1– and Chl triplet formation;
Energy migration from TChl to O2 and production of singlet oxygen 1O2;
Superoxide anion radical and H2O2 production in Mehler reaction;
Fenton reaction (OH• formation as result of interaction of H2O2 with reduced FeS-clusters);
Destruction of FeS-clusters by OH ;
Inactive FeS-clusters induce the conformational changes of PS1 core complex proteins facilitating its access for proteases;
Degradation of PsaB and PsaA gene products and release of 45 kDa and 51kDa proteins;
Processes (8) and (10) result PS1 photoinhibition
The eventual effect of the abiotic stress on plant growth and crop productivity is a result not only of the extent of the damage but also on the capacity for recovery after the damage has taken place. Although the recovery and repair of PSII after photoinhibition have been a subject of many studies [115, 116, 117], there is very little known about the recovery and repair of PSI. Teicher et. al. [118] showed that PSI recovery is a very slow process, which may take several days even under optimal conditions in field-grown barley. A more recent study showed that PSI damage in cucumber is not even completely reversible [119]
The few previous studies have not shown whether PSI repair is similar to PSII repair where one particular subunit, D1, is specifically remade whereas the rest of the complex is reused [120]. Clearly, the PSI repair process must involve some protein turnover but it is not known whether the breakdown that is observed during photodamage is caused directly by the damage or is part of the recovery process.
Light are highly unpredictable resource for plants and the changes in growth irradiance induce several changes in biochemical and molecular composition of the plant cell. Murchie et al. [121] showed that there are 99-light responsive genes which were down regulated and 130 were up-regulated in rice during light treatment. Majority of these genes showed reduced levels of expression in response to high light, whereas stress related genes showed increased level of expression. In order to avoid over-excitation of chlorophyll protein complexes and photooxidation, a regulated degradation of LHC was observed in rice leaves along with a decline in CP-24, PSI genes and a 10 kD PSII gene was also noticed under high light [121].
PS I has long been reported to be less affected than PSII by high light [105]. PSI in isolated thylakoid membranes was inactivated by high light [122]. Since PSI is the terminal electron carrier in the chloroplast, it was identified as a major site producing ROS and shown to be closely associated with ROS-scavenging systems in the chloroplast [123]. The role of ROS inactivating PSI reaction center and degradation of psaA and psaB under high light conditions has been studied [124]. Very recently, Jiao et al [125] demonstrated that high light stress readily photoinhibited PSI, following the loss of psaC as well as degradation of PSI reaction center proteins (psaA and psaB). The findings suggest that PSI photoinhibition can be a limiting factor in crop productivity under high light.
Several studies demonstrated that thylakoid memebrane proteins were affected by salt stress. In
A few reports have shown the effects of metals on the activity of photosystem I (PSI) and some of them was controversial. Neelam and Rai [133] reported that cadmium treatment inhibits PSI activity in
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