PSBP-DOMAIN PROTEIN1, a Nuclear-Encoded Thylakoid Lumenal Protein, Is Essential for Photosystem I Assembly in <i>Arabidopsis</i>

Liu, Jun; Yang, Huixia; Lu, Qingtao; Wen, Xiaopeng; Chen, Fan; Peng, Lianwei; Zhang, Lixin; Lu, Congming

doi:10.1105/tpc.112.106542

Cited by 116 publications

(131 citation statements)

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“…Immunolocalization and trypsin treatment of intact thylakoids were carried out as previously described (44). Subfractionation of thylakoids into grana margin, grana core, and stroma lamellae was performed as described in ref.…”

Section: Methodsmentioning

confidence: 99%

“…The light-induced in vivo absorbance changes of P700 at 820 nm were measured as described by Liu et al (44).…”

Section: Methodsmentioning

confidence: 99%

“…For BN-PAGE analysis, preparation and solubilization of intact thylakoids were performed as previously described (44). Electrophoresis was carried out by using Native PAGE Novex4-16% Bis-Tris mini gel and XCellSureLock minicell at 4°C (Thermo Fisher Scientific).…”

Section: Methodsmentioning

confidence: 99%

“…Thus far, proteomic analyses identified more than 80 lumenal thylakoid proteins in Arabidopsis (35, 36), with functions described for very few (23,44). We used a network approach to find lumenal proteins of unknown function coregulated with previously characterized lumenal photosynthetic regulatory factors (23,24) and identified MPH2 as matching the search criteria.…”

Section: Network Analysis Identified Mph2 As a Thylakoid Lumenal Psiimentioning

confidence: 99%

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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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Section: Methodsmentioning

confidence: 99%

“…The light-induced in vivo absorbance changes of P700 at 820 nm were measured as described by Liu et al (44).…”

Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Section: Network Analysis Identified Mph2 As a Thylakoid Lumenal Psiimentioning

confidence: 99%

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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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“…Indeed, other mutants with reduced photosynthetic efficiency also displayed reduced growth and development. 14,[19][20][21] NFU2 is involved in assembly and transfer of 4Fe-4S and classic 2Fe-2S clusters and the nfu2 mutants displayed similar trends as the nfu3 mutants. 14 The nfu2 mutants had a »30% reduction in PSI activity (calculated from Fig.…”

Section: Nfu3 Is Essential To Overall Plant Fitnessmentioning

confidence: 88%

Chloroplastic iron-sulfur scaffold protein NFU3 is essential to overall plant fitness

Nath

O’Donnell

2017

Plant Signaling & Behavior

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A previous study showed that Nitrogen-Fixing-subunit-U-type protein NFU3 may act an iron-sulfur scaffold protein in the assembly and transfer of 4Fe-4S and 3Fe-4S clusters in the chloroplast. Examples of 4Fe-4S and 3Fe-4S-requiring proteins and complexes include Photosystem I (PSI), NAD(P)H dehydrogenase, and ferredoxin-dependent glutamine oxoglutarate aminotransferases. In this paper, the authors provided additional evidence for the role of NFU3 in 4Fe-4S and 3Fe-4S cluster assembly and transfer, as well as its role in overall plant fitness. Confocal microscopic analysis of the fluorescently-tagged NFU3 protein confirmed the chloroplast localization of the NFU3 protein. Detailed analysis of chlorophyll fluorescence data revealed that a substantial increase in minimal fluorescence is the primary contributor to the decrease in PSII maximum photochemical efficiency observed in the nfu3 mutants. The substantial increase in minimal fluorescence in the nfu3 mutants is probably the result of an impaired PSI function, blockage of electron flow from PSII to PSI, and over-accumulation of reduced plastoquinone at the acceptor side of PSII. Analyses of seed morphology and germination showed that NFU3 is essential to seed development and germination, in addition to plant growth, development, and flowering. In summary, NFU3 has wide-ranging effects on many biologic processes and is therefore important to overall plant fitness. NFU3 may exert these effects by modulating the availability of 4Fe-4S and 3Fe-4S clusters to 4Fe-4S and 3Fe-4S-requiring proteins and complexes involved in various biologic processes.

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PALE‐GREEN LEAF 1, a rice cpSRP54 protein, is essential for the assembly of the PSI‐LHCI supercomplex

Gao

Xia

et al. 2022

Plant Direct

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Although photosynthetic multiprotein complexes have received major attention, our knowledge about the assembly of these proteins into functional complexes in plants is still limited. In the present study, we have identified a chlorophyll‐deficient mutant, pale ‐ green leaf 1 ( pgl1 ), in rice that displays abnormally developed chloroplasts. Map‐based cloning of this gene revealed that OsPGL1 encodes a chloroplast targeted protein homologous to the 54‐kDa subunit of the signal recognition particle (cpSRP54). Immunoblot analysis revealed that the accumulation of the PSI core proteins PsaA and PsaB, subunits from the ATP synthase, cytochrome, and light‐harvesting complex (LHC) is dramatically reduced in pgl1 . Blue native gel analysis of thylakoid membrane proteins showed the existence of an extra band in the pgl1 mutant, which located between the dimeric PSII/PSI‐LHCI and the monomeric PSII. Immunodetection after 2D separation indicated that the extra band consists of the proteins from the PSI core complex. Measurements of chlorophyll fluorescence at 77 K further confirmed that PSI, rather than PSII, was primarily impaired in the pgl1 mutant. These results suggest that OsPGL1 might act as a molecular chaperone that is required for the efficient assembly and specific integration of the peripheral LHCI proteins into the PSI core complex in rice.

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PSBP-DOMAIN PROTEIN1, a Nuclear-Encoded Thylakoid Lumenal Protein, Is Essential for Photosystem I Assembly in Arabidopsis

Cited by 116 publications

References 50 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

Chloroplastic iron-sulfur scaffold protein NFU3 is essential to overall plant fitness

PALE‐GREEN LEAF 1, a rice cpSRP54 protein, is essential for the assembly of the PSI‐LHCI supercomplex

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