Formation of DEG5 and DEG8 Complexes and Their Involvement in the Degradation of Photodamaged Photosystem II Reaction Center D1 Protein in <i>Arabidopsis</i>

Sun, Xuwu; Peng, Lianwei; Guo, J.; Chi, Wei; Ma, Jinfang; Lu, Congming; Zhang, Lixin

doi:10.1105/tpc.106.049510

Cited by 175 publications

(202 citation statements)

References 62 publications

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“…S14 A and B), as previously reported (30,31,42,43). In contrast, these mutants displayed reduced growth and PSII activity in the greenhouse (SI Appendix, Fig.…”

Section: Mph2 Promotes Psii Protein Subunit Turnover and Interacts Wisupporting

confidence: 57%

A chloroplast thylakoid lumen protein is required for proper photosynthetic acclimation of plants under fluctuating light environments

Liu

Last

2017

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

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Despite our increasingly sophisticated understanding of mechanisms ensuring efficient photosynthesis under laboratory-controlled light conditions, less is known about the regulation of photosynthesis under fluctuating light. This is important because-in naturephotosynthetic organisms experience rapid and extreme changes in sunlight, potentially causing deleterious effects on photosynthetic efficiency and productivity. Here we report that the chloroplast thylakoid lumenal protein MAINTENANCE OF PHOTOSYSTEM II UNDER HIGH LIGHT 2 (MPH2; encoded by At4g02530) is required for growth acclimation of Arabidopsis thaliana plants under controlled photoinhibitory light and fluctuating light environments. Evidence is presented that mph2 mutant light stress susceptibility results from a defect in photosystem II (PSII) repair, and our results are consistent with the hypothesis that MPH2 is involved in disassembling monomeric complexes during regeneration of dimeric functional PSII supercomplexes. Moreover, mph2-and previously characterized PSII repair-defective mutants-exhibited reduced growth under fluctuating light conditions, while PSII photoprotection-impaired mutants did not. These findings suggest that repair is not only required for PSII maintenance under static high-irradiance light conditions but is also a regulatory mechanism facilitating photosynthetic adaptation under fluctuating light environments. This work has implications for improvement of agricultural plant productivity through engineering PSII repair.fluctuating light | photosynthesis | photosystem II repair | photoprotection | chloroplast thylakoid lumen

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“…S14 A and B), as previously reported (30,31,42,43). In contrast, these mutants displayed reduced growth and PSII activity in the greenhouse (SI Appendix, Fig.…”

Section: Mph2 Promotes Psii Protein Subunit Turnover and Interacts Wisupporting

confidence: 57%

A chloroplast thylakoid lumen protein is required for proper photosynthetic acclimation of plants under fluctuating light environments

Liu

Last

2017

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

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“…We examined several available Arabidopsis mutant lines deficient in the chloroplast proteases FtsH2, FtsH5 (Kato et al, 2009), Deg2 (Huesgen et al, 2006), Deg5, Deg8 (Sun et al, 2007), and ClpR1 (Stanne et al, 2009) after a shift from blue light to far-red light. Some of these proteases act on the stromal side of the thylakoid membrane while others act on the lumen side or in the stroma.…”

Section: Resultsmentioning

confidence: 99%

The Phosphorylation Status of the Chloroplast Protein Kinase STN7 of Arabidopsis Affects Its Turnover

et al. 2011

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The chloroplast serine-threonine protein kinase STN7 of Arabidopsis (Arabidopsis thaliana) is required for the phosphorylation of the light-harvesting system of photosystem II and for state transitions, a process that allows the photosynthetic machinery to balance the light excitation energy between photosystem II and photosystem I and thereby to optimize the photosynthetic yield. Because the STN7 protein kinase of Arabidopsis is known to be phosphorylated at four serine-threonine residues, we have changed these residues by site-directed mutagenesis to alanine (STN7-4A) or aspartic acid (STN7-4D) to assess the role of these phosphorylation events. The corresponding mutants were still able to phosphorylate the light-harvesting system of photosystem II and to perform state transitions. Moreover, we noticed a marked decrease in the level of the STN7 kinase in the wild-type strain under prolonged state 1 conditions that no longer occurs in the STN7-4D mutant. The results suggest a possible role of phosphorylation of the STN7 kinase in regulating its turnover.

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“…Immunolocalization Studies-The localization of the LPA19 proteins were studied essentially as previously described (43). For the protease protection assay, the Arabidopsis thylakoid membrane samples (0.1 mg chlorophyll/ml) were each sonicated three times for 15 s on ice.…”

Section: Methodsmentioning

confidence: 99%

LPA19, a Psb27 Homolog in Arabidopsis thaliana, Facilitates D1 Protein Precursor Processing during PSII Biogenesis

Wei

Guo

Ouyang

et al. 2010

Journal of Biological Chemistry

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The biogenesis and assembly of photosystem II (PSII) are mainly regulated by the nuclear-encoded factors. To further identify the novel components involved in PSII biogenesis, we isolated and characterized a high chlorophyll fluorescence low psii accumulation19 (lpa19) mutant, which is defective in PSII biogenesis. LPA19 encodes a Psb27 homolog (At1g05385). Interestingly, another Psb27 homolog (At1g03600) in Arabidopsis was revealed to be required for the efficient repair of photodamaged PSII. These results suggest that the Psb27 homologs play distinct functions in PSII biogenesis and repair in Arabidopsis. Chloroplast protein labeling assays showed that the C-terminal processing of D1 in the lpa19 mutant was impaired. Protein overlay assays provided evidence that LPA19 interacts with D1, and coimmunoprecipitation analysis demonstrated that LPA19 interacts with mature D1 (mD1) and precursor D1 (pD1). Moreover, LPA19 protein was shown to specifically interact with the soluble C terminus present in the precursor and mature D1 through yeast two-hybrid analyses. Thus, these studies suggest that LPA19 is involved in facilitating the D1 precursor protein processing in Arabidopsis. Photosystem II (PSII),2 which catalyzes light-driven water oxidation and plastoquinone reduction, is a large pigment-protein complex found in the thylakoid membranes of cyanobacteria and chloroplasts. In higher plants, PSII contains more than 20 subunits including both integral and peripheral proteins (1, 2). The PSII reaction center proteins D1 and D2 bind most of the redox components essential for primary charge separation. Light energy transfer to the PSII reaction center is mediated by the intrinsic chlorophyll a-binding proteins, CP47 and CP43. The oxygen evolving complex, located on the luminal side of PSII, consists of a manganese cluster and several extrinsic proteins (3-6).

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Formation of DEG5 and DEG8 Complexes and Their Involvement in the Degradation of Photodamaged Photosystem II Reaction Center D1 Protein in Arabidopsis

Cited by 175 publications

References 62 publications

A chloroplast thylakoid lumen protein is required for proper photosynthetic acclimation of plants under fluctuating light environments

A chloroplast thylakoid lumen protein is required for proper photosynthetic acclimation of plants under fluctuating light environments

The Phosphorylation Status of the Chloroplast Protein Kinase STN7 of Arabidopsis Affects Its Turnover

LPA19, a Psb27 Homolog in Arabidopsis thaliana, Facilitates D1 Protein Precursor Processing during PSII Biogenesis

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