The extrinsic 33 kDa polypeptide of the oxygen-evolving complex of photosystem II is a putative calcium-binding protein and is encoded by a multi-gene family in pea

Wales, Richard; Newman, Barbara; Pappin, Darryl; Gray, John C.

doi:10.1007/bf00017583

Cited by 79 publications

(57 citation statements)

References 60 publications

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“…This was suggested originally by Wales et al (1989). Recently, Kruk et al (2003) presented evidence that spinach PsbO could bind Ca 2+ and La 3+ ions with a K d of about 10 lM.…”

Section: Introductionmentioning

confidence: 75%

The PSII calcium site revisited

2007

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Oxidation of H 2 O by photosystem II is a unique redox reaction in that it requires Ca 2+ as well as Cl -as obligatory activators/cofactors of the reaction, which is catalyzed by Mn atoms. The properties of the binding site for Ca 2+ in this reaction resemble those of other Ca 2+ binding proteins, and recent X-ray structural data confirm that the metal is in fact ligated at least in part by amino acid side chain oxo anions. Removal of Ca 2+ blocks water oxidation chemistry at an early stage in the cycle of redox reactions that result in O-O bond formation, and the intimate involvement of Ca 2+ in this reaction that is implied by this result is confirmed by an ever-improving set of crystal structures of the cyanobacterial enzyme. Here, we revisit the photosystem II Ca 2+ site, in part to discuss the additional information that has appeared since our earlier review of this subject (van Gorkom HJ, Yocum CF In: Wydrzynski TJ, Satoh K (eds) Photosystem II: the light-driven water:plastoquinone oxidoreductase), and also to reexamine earlier data, which lead us to conclude that all S-state transitions require Ca 2+ .

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“…This was suggested originally by Wales et al (1989). Recently, Kruk et al (2003) presented evidence that spinach PsbO could bind Ca 2+ and La 3+ ions with a K d of about 10 lM.…”

Section: Introductionmentioning

confidence: 75%

The PSII calcium site revisited

2007

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“…Isoforms can be expected for several of the photosynthetic proteins, because multigene families have been reported in pea, spinach, and tobacco for OEC23 (e.g., Hua et al, 1992), OEC33 (e.g., Wales et al, 1989), and ferredoxin-NADPH reductase (e.g., Gozzer et al, 1997). Post-translational modifications are likely to occur not only through phosphorylation but also by post-translational methylation (e.g., of RbcS; Grimm et al, 1997), carbamylation (e.g., for RbcS and RbcL; Smith et al, 1988), glycosylation (e.g., for CF 1 ; Maione and Jagendorf, 1984), and palmitoylation (e.g., for the D1 protein; Mattoo and Edelman, 1987).…”

Section: Total Number Of Peripheral and Lumenal Thylakoid Proteinsmentioning

confidence: 99%

Proteomics of the Chloroplast: Systematic Identification and Targeting Analysis of Lumenal and Peripheral Thylakoid Proteins

Peltier

Friso

Kalume³

et al. 2000

Plant Cell

334

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The soluble and peripheral proteins in the thylakoids of pea were systematically analyzed by using two-dimensional electrophoresis, mass spectrometry, and N-terminal Edman sequencing, followed by database searching. After correcting to eliminate possible isoforms and post-translational modifications, we estimated that there are at least 200 to 230 different lumenal and peripheral proteins. Sixty-one proteins were identified; for 33 of these proteins, a clear function or functional domain could be identified, whereas for 10 proteins, no function could be assigned. For 18 proteins, no expressed sequence tag or full-length gene could be identified in the databases, despite experimental determination of a significant amount of amino acid sequence. Nine previously unidentified proteins with lumenal transit peptides are presented along with their full-length genes; seven of these proteins possess the twin arginine motif that is characteristic for substrates of the TAT pathway. Logoplots were used to provide a detailed analysis of the lumenal targeting signals, and all nuclear-encoded proteins identified on the two-dimensional gels were used to test predictions for chloroplast localization and transit peptides made by the software programs ChloroP, PSORT, and SignalP. A combination of these three programs was found to provide a useful tool for evaluating chloroplast localization and transit peptides and also could reveal possible alternative processing sites and dual targeting. The potential of proteomics for plant biology and homology-based searching with mass spectrometry data is discussed.

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“…Similar heterogeneities have been observed for other plant genes (Schaller et al 1991). So far isoforms of the 33 kDa protein have only been characterized in pea (Wales et al 1989). A comparison of the tomato 33 kDa cDNA with a cDNA fragment isolated by Ko et al (1990) from tomato indicates the existence of isoforms of the 33 kDa protein in tomato (Fig.…”

mentioning

confidence: 99%

“…To extend the cDNA sequence anchored PCR was performed and the resulting PCR fragments were subcloned and sequenced. The sequence of one PCR fragment which was identical as 92 (92) 82 (88) 75 (84) 69 (80) 53 (66) 25 (43) 66 (72) 45 ( (Tyagi et al 1987), P. sativum (Wales et al 1989), A. thaliana (Ko et al 1990), T. aestivum (Meadows et al 1991), C. reinhardtii (Mayfield et al 1989), Anabaena sp. (Borthakur and Haselkorn 1989), Synechocystis sp.…”

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confidence: 99%

The 33 kDa Protein of the Oxygen-Evolving Complex: a Multi-Gene Family in Tomato

1993

Plant and Cell Physiology

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A cDNA was isolated by chance from tomato which had a high similarity to a cDNA clone from potato known to code for the 33 kDa protein of the oxygen-evolving complex [van Spanje et al. (1991) Plant Mol. Biol. 17: 157]. The sequence of a previously described partial cDNA clone from tomato [Ko et al. (1990) Plant Mol. Biol. 14: 217] which has also a high similarity but is not identical to the sequence described here indicates that tomato contains at least two genes coding for 33 kDa proteins per haploid genome. This conclusion is supported by Southern blot analysis. The tissue specific expression of the corresponding genes is described.Key words: Multi-gene family -Oxygen-evolving complex -Photosynthesis -Tomato (Lycopersicon esculentum L.).In plants, oxygen is evolved at the inner face of the thylakoid membrane in the so-called OEC, which is part of PSII. Three extrinsic luminal membrane proteins, the so called 33 kDa, 23 kDa and 16 kDa proteins, are involved in the manganese-dependent water splitting reaction (Andersson et al. 1984). The detailed structure of the OEC and the molecular mechanism of the reaction are not yet known (Babcock et al. 1989, Rutherford 1989. The 23 kDa and 16 kDa proteins function in the stabilization and regulation of the complex. The 33 kDa protein seems to be a constituent of the Mn-cluster and is directly involved in O 2 -generation. The 33 kDa proteins from plants show high structural and functional homologies to the 33 kDa manganesestabilizing polypeptide of the PSII from cyanobacteria (Koike and Inoue 1985). This 33 kDa protein is one of four well characterized proteins of the thylakoid lumen. Like plastocyanin and the other extrinsic components of the OEC, the 33 kDa protein is a nuclear-encoded protein (Westhoff et al. 1985, Jansen et al. 1987). The higher molecular weight precursors are synthesized in the cytosol and processed to the mature form by proteolytic cleavage while Abbreviations: bp, base pair; OEC, oxygen-evolving complex; PCR, polymerase chain reaction; pfu, plaque forming units; RT, room temperature.

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The extrinsic 33 kDa polypeptide of the oxygen-evolving complex of photosystem II is a putative calcium-binding protein and is encoded by a multi-gene family in pea

Cited by 79 publications

References 60 publications

The PSII calcium site revisited

The PSII calcium site revisited

Proteomics of the Chloroplast: Systematic Identification and Targeting Analysis of Lumenal and Peripheral Thylakoid Proteins

The 33 kDa Protein of the Oxygen-Evolving Complex: a Multi-Gene Family in Tomato

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