Recombinant Liriodendron tulipifera Photosystem II reaction center protein H (psbH)

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Description

Introduction to psbH in Photosystem II

Photosystem II (PSII) reaction center protein H (psbH) is a critical component of the photosynthetic machinery in plants, including Liriodendron tulipifera. This 10 kDa phosphoprotein stabilizes the PSII complex and regulates electron transport during light-dependent reactions . The recombinant form of psbH is engineered for research applications, enabling studies into its structural and functional roles in photosynthesis.

Production and Biochemical Characteristics

ParameterDetails
Expression RegionAmino acids 2–73 (partial sequence)
Uniprot IDQ0G9J0
AA SequenceATQTVEGSSRSGPRRTITGDLLKPLNSEYGKVAPGWGTTPFMGVAMALFAIFLSIILEIY NSSVLLDGISMS
Tag InfoDetermined during production (e.g., His-tag or other affinity tags)
Storage BufferTris-based buffer with 50% glycerol, pH optimized for stability
PurityNot explicitly stated; inferred from standard recombinant protein protocols
Storage Conditions-20°C or -80°C; avoid repeated freezing/thawing cycles

The protein is sold as a 50 µg vial, priced at €1,411.00, and is primarily marketed for immunoassay applications (e.g., ELISA) .

Applications in Research

Recombinant psbH from L. tulipifera is utilized in:

  • ELISA Kits: As a component for detecting psbH antibodies or studying protein-protein interactions in photosynthesis research .

  • Structural Studies: Investigating phosphorylation patterns and interactions with other PSII subunits.

  • Comparative Biochemistry: Analyzing evolutionary conservation of psbH across plant species.

Research Gaps and Future Directions

While the recombinant psbH from L. tulipifera is well-characterized for immunoassays, further studies are needed to:

  • Elucidate Functional Roles: Investigate its phosphoprotein dynamics in L. tulipifera under stress conditions.

  • Expand Applications: Explore its use in structural biology (e.g., X-ray crystallography) or mutant studies.

This review synthesizes available data on recombinant L. tulipifera psbH, highlighting its biochemical properties and research potential. Future work should leverage this protein to advance understanding of photosynthetic regulation in magnoliids.

Product Specs

Form
Lyophilized powder
Note: We prioritize shipping the format readily available in our inventory. However, if you have specific format requirements, please indicate them during order placement, and we will fulfill your request.
Lead Time
Delivery time may vary depending on the purchase method and location. Kindly consult your local distributors for specific delivery estimates.
Note: All our proteins are shipped with standard blue ice packs by default. If you require dry ice shipping, please inform us in advance, as additional fees will apply.
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Reconstitution
We recommend centrifuging the vial briefly before opening to ensure the contents settle at the bottom. Reconstitute the protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. We recommend adding 5-50% glycerol (final concentration) and aliquoting for long-term storage at -20°C/-80°C. Our default final glycerol concentration is 50%. Customers may use this as a reference.
Shelf Life
Shelf life is influenced by various factors, including storage conditions, buffer components, temperature, and the inherent stability of the protein.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Storage Condition
Store at -20°C/-80°C upon receipt, aliquoting is necessary for multiple uses. Avoid repeated freeze-thaw cycles.
Tag Info
Tag type will be determined during the manufacturing process.
The tag type is determined during the production process. If you have a specific tag type in mind, please inform us, and we will prioritize developing the specified tag.
Synonyms
psbH; Photosystem II reaction center protein H; PSII-H; Photosystem II 10 kDa phosphoprotein
Buffer Before Lyophilization
Tris/PBS-based buffer, 6% Trehalose.
Datasheet
Please contact us to get it.
Expression Region
2-73
Protein Length
Full Length of Mature Protein
Species
Liriodendron tulipifera (Tuliptree) (Tulip poplar)
Target Names
psbH
Target Protein Sequence
ATQTVEGSSRSGPRRTITGDLLKPLNSEYGKVAPGWGTTPFMGVAMALFAIFLSIILEIY NSSVLLDGISMS
Uniprot No.

Target Background

Function
Photosystem II reaction center protein H (psbH) is an integral component of the core complex in photosystem II (PSII), playing a crucial role in its stability and assembly. PSII is a light-driven water:plastoquinone oxidoreductase that utilizes light energy to extract electrons from H(2)O, generating O(2) and a proton gradient, which subsequently drives ATP formation. It comprises a core antenna complex responsible for capturing photons and an electron transfer chain that converts photonic excitation into charge separation.
Protein Families
PsbH family
Subcellular Location
Plastid, chloroplast thylakoid membrane; Single-pass membrane protein.

Q&A

Basic Research Questions

  • What is the fundamental role of psbH in photosystem II function?

    The psbH protein serves as a small but critical subunit of the photosystem II (PSII) complex, identified as a 6-kDa protein in the PSII core and subcore components. Research demonstrates that psbH is essential for maintaining structural integrity of PSII, particularly in stabilizing the attachment of CP47 to the D1-D2 heterodimer . Additionally, psbH plays a significant role in bicarbonate binding on the PSII acceptor side, which directly impacts electron transport efficiency. Studies using psbH-deficient mutants have shown that without this protein, PSII exhibits increased sensitivity to environmental stressors and reduced photosynthetic efficiency .

  • How does the psbH sequence in Liriodendron tulipifera compare to model organisms?

    While specific sequence data for Liriodendron tulipifera psbH is limited in current literature, comparative analysis with other plant species reveals several conserved domains essential for PSII function. Conservation analysis typically shows higher preservation in functional regions directly involved in protein-protein interactions and structural stability. Researchers should employ standard sequence alignment tools comparing the tulip tree psbH with well-characterized homologs from model organisms such as Arabidopsis thaliana or Spinacia oleracea. For recombinant expression studies, these conserved regions must be maintained while considering tulip tree-specific sequence variations that may influence protein folding and integration.

  • What expression systems are most suitable for recombinant Liriodendron tulipifera psbH production?

    For recombinant expression of Liriodendron tulipifera psbH, several expression systems warrant consideration based on research objectives:

    Expression SystemAdvantagesLimitationsBest Applications
    E. coliRapid growth, high yield, cost-effectiveMay lack proper folding for membrane proteinsInitial characterization, antibody production
    Cyanobacterial systemsNative-like membrane environment, functional validationSlower growth, specialized expertise requiredFunctional studies, structural analysis
    Plant cell culturePost-translational modifications, proper foldingLower yields, longer cultivation timesInteraction studies, physiological relevance
    Cell-free systemsMembrane protein compatibility, rapid resultsHigher cost, optimization requiredDifficult-to-express variants, rapid screening

    For functional studies, cyanobacterial expression systems like Synechocystis PCC 6803 offer particular advantages as they provide a native-like thylakoid membrane environment essential for proper psbH integration and function .

Advanced Research Questions

  • How do mutations in the psbH gene affect PSII stability and electron transport in Liriodendron tulipifera?

    Mutations in psbH significantly impact PSII stability and electron transport kinetics. Based on research with model organisms, the absence of psbH leads to several observable phenomena that would likely apply to Liriodendron tulipifera:

    • Weakened attachment of CP47 to the D1-D2 heterodimer, resulting in dissociation during isolation procedures

    • Decreased QA- reoxidation rates under CO2-depleted conditions, indicating compromised electron transport

    • Increased HCO3- dependency for maintaining PSII activity under illumination

    • Enhanced susceptibility to photodamage, leading to D1 protein oxidation, fragmentation, and cross-linking

    For investigating these effects in Liriodendron tulipifera specifically, researchers should employ site-directed mutagenesis of conserved residues followed by functional assays measuring oxygen evolution, chlorophyll fluorescence kinetics, and protein stability under varying light and CO2 conditions.

  • What experimental approaches best characterize psbH-mediated protection against photodamage in Liriodendron tulipifera?

    To effectively characterize psbH's role in photoprotection within Liriodendron tulipifera, researchers should implement a parallel design experimental approach where:

    Experiment 1: Establish baseline photodamage susceptibility by exposing wild-type samples to controlled high-light treatments while measuring:

    • D1 protein turnover rates using pulse-chase radiolabeling

    • Reactive oxygen species (ROS) production with fluorescent probes

    • PSII quantum yield through PAM fluorometry

    Experiment 2: Compare these parameters in:

    • psbH knockdown/knockout samples (using RNAi or CRISPR)

    • Complemented lines expressing modified psbH variants

    • Samples under different bicarbonate concentrations

    This parallel experimental design allows for direct comparison between conditions while controlling for variables that might affect photodamage independently . The approach provides stronger identification power than single-experiment designs by allowing researchers to isolate the causal pathway through which psbH mediates photoprotection .

  • How does psbH phosphorylation status influence PSII repair cycle in Liriodendron tulipifera under environmental stress?

    Although no direct evidence for psbH phosphorylation was found in some studies with cyanobacteria , other research suggests that in higher plants, psbH undergoes reversible phosphorylation under varying light conditions. For Liriodendron tulipifera, understanding this regulatory mechanism requires a systematic approach:

    1. First, characterize phosphorylation sites using mass spectrometry of isolated PSII complexes under different environmental conditions

    2. Generate phosphomimetic (Ser/Thr → Asp/Glu) and phospho-null (Ser/Thr → Ala) variants via site-directed mutagenesis

    3. Assess PSII repair cycle efficiency through D1 turnover rates and assembly/disassembly kinetics

    4. Quantify stress tolerance by measuring photosynthetic parameters under temperature, drought, and high-light stressors

    Researchers should apply a crossover experimental design where samples are sequentially subjected to different stressors with recovery periods, allowing for assessment of how phosphorylation state influences repair dynamics across varying conditions .

Data Analysis and Interpretation

  • How should researchers interpret contradictory findings regarding psbH function between in vitro and in vivo experiments?

    Contradictions between in vitro and in vivo findings require systematic reconciliation through:

    1. Mechanistic examination: Identify whether discrepancies arise from:

      • Different redox environments affecting protein-protein interactions

      • Absence of regulatory factors present only in intact systems

      • Altered membrane composition influencing protein complex stability

    2. Validation through intermediate systems:

      • Thylakoid membrane preparations (semi-intact system)

      • Isolated chloroplasts (organellar context)

      • Protoplast cultures (cellular context but manipulable)

    3. Implementation of causal mediation analysis:

      • Apply statistical frameworks to decompose total effects into direct and indirect components

      • Estimate average natural indirect effects through experimental designs that randomize both treatment and mediator variables

    When findings conflict, researchers should prioritize results from experimental designs that provide stronger identification power, such as parallel or crossover designs over single-experiment approaches .

  • What are the best approaches for analyzing psbH interaction networks in Liriodendron tulipifera PSII complexes?

    For comprehensive analysis of psbH interaction networks:

    1. Primary interaction identification:

      • Cross-linking mass spectrometry (XL-MS) to capture direct protein-protein contacts

      • Co-immunoprecipitation with anti-psbH antibodies followed by proteomics

      • Yeast two-hybrid or split-GFP assays for binary interactions

    2. Functional validation of interactions:

      • Mutagenesis of putative interaction interfaces

      • Competition assays with synthetic peptides corresponding to interaction domains

      • In vitro reconstitution with purified components

    3. Temporal dynamics analysis:

      • Pulse-chase experiments to track assembly/disassembly kinetics

      • Time-resolved crosslinking under various physiological conditions

    4. Network visualization and analysis:

      • Construct interaction networks with weighted edges based on interaction strength

      • Apply centrality measures to identify key nodes in the PSII interactome

      • Compare networks under stress vs. optimal conditions

    These approaches should be integrated to develop a comprehensive model of how psbH mediates its effects through multiple protein-protein interactions within the PSII complex.

  • How can transcriptomic and proteomic data be integrated to understand psbH regulation in Liriodendron tulipifera under environmental stress?

    Effective multi-omics integration for understanding psbH regulation requires:

    Data TypeKey MeasurementsIntegration Approach
    TranscriptomicspsbH mRNA expression levels, alternative splicing eventsTemporal correlation with protein abundance
    ProteomicspsbH protein levels, post-translational modificationsQuantitative analysis of protein/transcript ratios
    MetabolomicsPhotosynthetic intermediates, ROS indicatorsPathway analysis linking metabolic changes to psbH function
    Physiological dataPhotosynthetic efficiency (Fv/Fm), electron transport ratesCorrelation with molecular markers

    For datasets with complex relationships, implement:

    1. Advanced statistical modeling approaches that account for non-linear relationships between transcript and protein levels

    2. Machine learning methods optimized for tabular data integration, such as gradient-boosted decision trees or foundation models like TabPFN

    3. Network inference algorithms to identify regulatory hubs controlling psbH expression and activity

    This integrated analysis allows researchers to distinguish between transcriptional, post-transcriptional, and post-translational regulation of psbH under different environmental stressors.

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