Two sites of primary degradation of the D1‐protein induced by acceptor or donor side photo‐inhibition in photosystem II core complexes

Rivas, Javier De Las; Andersson, Bertil; Barber, James

doi:10.1016/0014-5793(92)80250-k

Cited by 112 publications

(84 citation statements)

References 29 publications

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“…Our data demonstrate that, under our experimental conditions, the 18-kDa peptide arises from the C terminus of the D1 protein and includes the portions of the D-de loop bearing the antigenic determinants for the D-de loop antibody. A number of other laboratories, using a variety of experimental protocols, have observed a D1 fragment of similar apparent molecular mass (27)(28)(29). The higher molecular mass bands at 52 and 68 kDa are aggregates containing D1 and possibly other protein components.…”

Section: Resultsmentioning

confidence: 93%

Amino acid oxidation of the D1 and D2 proteins by oxygen radicals during photoinhibition of Photosystem II

Kale

Hebert

Frankel

et al. 2017

Proc. Natl. Acad. Sci. U.S.A.

132

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The Photosystem II reaction center is vulnerable to photoinhibition. The D1 and D2 proteins, lying at the core of the photosystem, are susceptible to oxidative modification by reactive oxygen species that are formed by the photosystem during illumination. Using spin probes and EPR spectroscopy, we have determined that both O 2 . The identification of specific amino acid residues oxidized by reactive oxygen species provides insights into the mechanism of damage to the D1 and D2 proteins under light stress.photosynthesis | Photosystem II | reactive oxygen species | photo inhibition | mass spectrometry P hotosystem II (PSII) functions as a water-plastoquinone oxidoreductase (1, 2) and is a thylakoid membrane pigmentprotein complex present in all oxygenic photosynthetic organisms (cyanobacteria, algae, and higher plants). Current high-resolution structures of thermophilic cyanobacterial PSII (3, 4), and lower resolution structures of the red algal (5) and higher plant photosystems (6), have been critically important in furthering our understanding of the molecular organization of PSII. Structurally, the PSII reaction center core is composed of five proteins: D1, D2, the α-and β-subunits of cytochrome b 559 , and PsbI. These components bind all of the redox-active cofactors of PSII.Excitation energy transfer and electron transport within PSII are unavoidably associated with production of reactive oxygen species (ROS) when the absorption of light by the chlorophyll antenna exceeds the capacity for energy utilization. Many mechanisms for ROS production have been proposed (for reviews, see refs. 7 and 8). Briefly, singlet oxygen ( 1 O 2 ) may be formed by excitation energy transfer from triplet chlorophylls (formed either by the change in orientation of the spin of an excited electron in the PSII antenna complex, or via charge recombination of the primary radical pair 3 [P 680 •+ Pheo •− ]) to O 2 (9, 10). ROS production by electron transport involves either the two-electron oxidation of water or the one-electron reduction of O 2 on the PSII electron donor and acceptor sides, respectively. On the PSII electron donor side, a twoelectron oxidation of water leads to the formation of hydrogen peroxide (H 2 O 2 ), which may be oxidized to the superoxide anion radical (O 2•−

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Section: Resultsmentioning

confidence: 93%

Amino acid oxidation of the D1 and D2 proteins by oxygen radicals during photoinhibition of Photosystem II

Kale

Hebert

Frankel

et al. 2017

Proc. Natl. Acad. Sci. U.S.A.

132

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“…Its breakdown products have been identified both in rive [27] and in vitro [10,11], and the existence of specific pathways for D1 degradation depending on whether donor or accepter side photoinhibition is involved, has been proven [17][18][19]. Accepter side photoinhibition is thought to produce cleavage in the hydrophobie loop connecting the 3rd and 4th transmembrane segments [27], whilst donor side photoinhihition probably leads to a cleavage in the loop connecting the 1st and 2nd and the 3rd and 4th transmembrane segments [15].…”

Section: Discussionmentioning

confidence: 99%

“…Some light-induced fragments have been isolated and characterized [15] and there is now agreement that degradation of the protein may proceed Abbreviat&ns: cyt, cytochrome; DBMIB, 5-dibromo-3-methyi-6-isopropyl-p-b~nzoquinone; PMSF, phenyl-methane-sulphonyl fluoride; PSII, photosystem 11; PVDF, polyvinylidene difiuoride; RCII, reaction center complex of photosystem It. along different pathways, depending on whether its degradation is triggered by damage at the donor or aeceptor sides [17][18][19]. Some photodegradation products of the D2 protein have also been detected [12,14].…”

Section: Introductionmentioning

confidence: 99%

Light‐induced degradation of D2 protein in isolated photosystem II reaction center complex

Barbato

Friso

Laureto³

et al. 1992

FEBS Letters

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When isolated photosystem I1 reaction centers from spinach are exposed to photoinhibitory light in the presence of an electron aceeptor, breakdown products of the D2 protein at 28, 25, 23, 18, 9, 5 and 4.5 kDa are detected by immunoblotting with a monospeeifie anti-D2 polyelonal antibody. In a time-course experi~i~ent the 23 and 4.5 kDa fragments show a transient appearance, whilst the others are photoaceumulated. The regions of the D2 protein containing tl~e cleavage sites tbr the 28 and 18 kDa photoindueed fragments have been identified. Significant degradation of D2 takes place only in the presence: of an electron aeceptor, and breakdown of the protein is partially prevented by serine-type proteas¢ inhibitors.

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“…Although light energy is a specific requirement for the production of stored chemical energy, too much light is known to inhibit photosynthesis and damage the photosynthetic apparatus (Kok, 1956;Kyle et al, 1984;Ohad et al, 1984). The main site of this inhibitory effect has been located in photosystem I1 (PSII; Powles, 1984), and has been linked to the turnover of one of the central reaction centre components, the D1 protein, which is the product of the psbA gene (Prasil et al, 1992;Barber and Andersson, 1992). It has also been shown that another reaction centre protein, which is encoded by the psbD gene, is degraded as a consequence of illumination with high light intensities (Schuster et al, 1988), although D2 is found to be relatively stable at low light levels (Gounaris et al, 1987).…”

mentioning

confidence: 99%

In vivo and in vitro photoinhibition reactions generate similar degradation fragments of D1 and D2 photosystem‐II reaction‐centre proteins

Shipton

Barber

1994

European Journal of Biochemistry

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Isolation of photosystem-I1 reaction centres from pea leaves after photoinhibitory treatment at low temperature (0-1 "C) has provided evidence for the mechanism of degradation of the D1 protein in vivo. These isolated reaction centres did not appear to be spectrally distinct from preparations obtained from control leaves that had not been photoinhibited. Breakdown fragments of both the D1 and D2 proteins were, however, found in preparations isolated from photoinhibited leaves, and showed similarities with those detected when isolated reaction centres were exposed to acceptorside photoinhibition. Analyses of the origin of D1 fragments indicated that the primary cleavage site of this protein was between transmembrane helices IV and V indicative of the acceptor-side mechanism for photoinhibition. The origins of other D1 protein fragments indicate that some donorside photoinhibition may also have occurred in vivo under the conditions employed. We have shown that the spectral and functional integrating of the isolated photosystem I1 reaction centre complex is resistant to proteolytic cleavage by trypsin. Use of a more non-specific protease (subtilisin), however, caused significant destabilisation of the special pair of chlorophylls constituting the primary electron donor, P680, with a consequential loss of functional activity. Thus, it is possible that specific cleavage of photosystem-I1 reaction-centre proteins may occur in vivo following photoinhibitory damage without a significant change in structural integrity, a conclusion supported by the finding that photodamaged and normal reaction centres were isolated together.

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Two sites of primary degradation of the D1‐protein induced by acceptor or donor side photo‐inhibition in photosystem II core complexes

Cited by 112 publications

References 29 publications

Amino acid oxidation of the D1 and D2 proteins by oxygen radicals during photoinhibition of Photosystem II

Amino acid oxidation of the D1 and D2 proteins by oxygen radicals during photoinhibition of Photosystem II

Light‐induced degradation of D2 protein in isolated photosystem II reaction center complex

In vivo and in vitro photoinhibition reactions generate similar degradation fragments of D1 and D2 photosystem‐II reaction‐centre proteins

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