Recombinant Oenothera elata subsp. hookeri Photosystem II reaction center protein Z (psbZ)

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Description

Production and Purification

The recombinant psbZ protein is produced via bacterial expression systems, optimized for high yield and purity:

ParameterSpecification
Host OrganismE. coli
FormLyophilized powder
Storage BufferTris/PBS-based buffer, 6% trehalose, pH 8.0
ReconstitutionDeionized sterile water (0.1–1.0 mg/mL), with 5–50% glycerol for stabilization
Shelf Life-20°C/-80°C (long-term), 4°C (short-term working aliquots)

Notes:

  • Repeated freeze-thaw cycles are discouraged to avoid degradation .

  • Trehalose and glycerol are used to enhance protein stability during storage .

Role in Photosystem II Assembly

psbZ is essential for PSII core assembly and stability. Studies in Oenothera hybrids highlight its role in chloroplast genome incompatibility under high light (HL) conditions:

  • Transcript Regulation: Under HL stress, psbZ transcript levels in incompatible hybrids (AB-I) are reduced, though this contributes minimally to the incompatibility phenotype compared to the psbB operon promoter region .

  • Protein Abundance: Western blot analyses show ~80% reduction in Cytb6f (a component of the cytochrome b6f complex) in AB-I hybrids under HL, but psbZ itself is not directly implicated in this reduction .

Evolutionary Context

Codon usage bias (CUB) studies in Oenothera plastomes reveal:

  • Mutational Pressure: GC3 and T3 contents correlate strongly with CUB, suggesting genetic drift and compositional constraints shape synonymous codon usage .

  • Weak Selection: Natural selection influences codon usage in psbZ and other PSII-related genes, though its role is less pronounced compared to mutational pressure .

Experimental Uses

  • Structural Studies: Recombinant psbZ is used to study PSII core interactions and photoprotection mechanisms.

  • Chloroplast Gene Regulation: Investigates light-dependent transcriptional control of psbZ and adjacent operons (e.g., psbB) .

Limitations

  • Post-Translational Modifications: E. coli-derived psbZ lacks chloroplast-specific modifications, which may affect functional studies .

Product Specs

Form
Lyophilized powder
Note: We will prioritize shipping the format currently in stock. However, if you have a specific format requirement, please indicate it in your order notes. We will fulfill your request if possible.
Lead Time
Delivery time may vary depending on the purchasing method and location. Please contact your local distributor for specific delivery details.
Note: Our proteins are shipped with standard blue ice packs. If you require dry ice shipping, please communicate with us in advance as additional fees will apply.
Notes
Avoid repeated freezing and thawing. 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 to 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 glycerol concentration is 50%. Customers can use this as a reference.
Shelf Life
Shelf life depends on factors including storage conditions, buffer composition, temperature, and the protein's inherent stability.
Generally, liquid forms have a shelf life of 6 months at -20°C/-80°C. Lyophilized forms have a shelf life of 12 months at -20°C/-80°C.
Storage Condition
Store at -20°C/-80°C upon receipt. Aliquot for multiple uses. Avoid repeated freeze-thaw cycles.
Tag Info
Tag type will be determined during the manufacturing process.
The tag type will be determined during production. If you have a specific tag type requirement, please inform us, and we will prioritize developing the specified tag.
Synonyms
psbZ; ycf9; Photosystem II reaction center protein Z; PSII-Z
Buffer Before Lyophilization
Tris/PBS-based buffer, 6% Trehalose.
Datasheet
Please contact us to get it.
Expression Region
1-62
Protein Length
full length protein
Species
Oenothera elata subsp. hookeri (Hooker's evening primrose) (Oenothera hookeri)
Target Names
psbZ
Target Protein Sequence
MTIAFQLAVFALIATSSLLLISVPVVFASPEGWSSNKNVVFSGTSLWIGLVFLVGILNSL IS
Uniprot No.

Target Background

Function
Controls the interaction of photosystem II (PSII) cores with the light-harvesting antenna.
Protein Families
PsbZ family
Subcellular Location
Plastid, chloroplast thylakoid membrane; Multi-pass membrane protein.

Q&A

What is Photosystem II reaction center protein Z (psbZ) and what is its role in photosynthesis?

Photosystem II reaction center protein Z (psbZ) is a small membrane protein component of the photosystem II complex, essential for photosynthetic electron transport in plants, algae, and cyanobacteria. It plays a critical role in maintaining optimal photosynthetic efficiency, particularly under varying light conditions. The protein helps stabilize the core architecture of photosystem II and facilitates electron transfer processes between photosystem II and downstream components of the photosynthetic electron transport chain. Research indicates that psbZ is involved in regulating energy distribution between photosystems and may contribute to photoprotection mechanisms in plants .

Why is Oenothera elata subsp. hookeri specifically used as a source for studying psbZ?

Oenothera elata subsp. hookeri (Hooker's evening primrose) has become an important model organism for studying photosynthetic proteins due to several key advantages:

  • The Oenothera genus exhibits unique genetic and plastome characteristics that make it particularly valuable for studying molecular mechanisms of speciation and plastid evolution .

  • The complete plastid chromosome of Oenothera elata subsp. hookeri has been fully sequenced (accession no. AJ271079.3), providing a comprehensive genetic foundation for protein studies .

  • This subspecies shows distinctive adaptation to various light conditions corresponding to its natural habitat in coastal and inland environments of California, from sea level up to 7,000 feet elevation .

  • The evening-blooming habit of this plant represents an interesting adaptation that may reflect specialized photosystem regulation mechanisms .

  • The relatively well-characterized genetics and availability of the species makes it an accessible model for comparative photosynthesis research .

What are the structural characteristics of psbZ from Oenothera elata subsp. hookeri?

The psbZ protein from Oenothera elata subsp. hookeri has the following structural characteristics:

  • It consists of 62 amino acids (full length: 1-62 aa)

  • Amino acid sequence: MTIAFQLAVFALIATSSLLLISVPVVFASPEGWSSNKNVVFSGTSLWIGLVFLVGILNSL IS

  • It is a transmembrane protein, with hydrophobic regions that anchor it within the thylakoid membrane

  • The protein contains characteristic motifs found in photosystem II reaction center proteins

  • It has a conserved structure compared to psbZ from other photosynthetic organisms, though with species-specific variations

  • The protein's folding and integration into the photosystem II complex is essential for its functional activity

How should I design a robust experiment to characterize the function of recombinant psbZ?

When designing experiments to characterize recombinant psbZ function, follow these methodological steps:

  • Define clear research questions and hypotheses: Formulate specific, testable hypotheses about psbZ function, such as its role in electron transport or interaction with other photosystem components .

  • Identify and define variables:

    • Independent variable: Treatment conditions (e.g., light intensity, recombinant psbZ concentration, presence of inhibitors)

    • Dependent variable: Measurable outcomes (e.g., electron transport rate, complex stability)

    • Controlled variables: pH, temperature, buffer composition, other photosystem components

  • Design multiple experimental approaches:

    • In vitro reconstitution with purified components

    • Complementation studies in psbZ-deficient systems

    • Comparative analysis with native protein

    • Structure-function analysis through site-directed mutagenesis

  • Include proper controls:

    • Negative control: Reactions without psbZ

    • Positive control: Reactions with native psbZ

    • Vehicle control: Buffer-only additions

    • Specificity control: Unrelated protein of similar size/properties

  • Ensure adequate replication:

    • Multiple technical replicates (minimum 3)

    • Multiple biological replicates (different protein preparations)

    • Statistical power analysis to determine appropriate sample size

  • Implement randomization and blinding where possible to minimize investigator bias .

  • Plan appropriate data collection and analysis methods prior to beginning experiments .

What methodological considerations are important when working with recombinant psbZ protein?

When working with recombinant psbZ, researchers should consider the following methodological factors:

  • Protein storage and handling:

    • Store lyophilized protein at -20°C/-80°C and avoid repeated freeze-thaw cycles

    • For working solutions, store aliquots at 4°C for up to one week

    • Reconstitute in appropriate buffer systems (typically Tris-based buffers at pH 8.0)

    • Consider including 50% glycerol for long-term storage stability

  • Reconstitution protocols:

    • Briefly centrifuge vials before opening to bring contents to the bottom

    • Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL

    • Allow complete dissolution before experimental use

  • Membrane protein challenges:

    • psbZ is a membrane protein requiring special handling to maintain native conformation

    • Consider inclusion of appropriate detergents or lipid environments

    • Monitor protein aggregation and precipitation

  • Quality control:

    • Verify protein purity via SDS-PAGE (should be >90%)

    • Confirm protein identity through Western blotting or mass spectrometry

    • Assess functional activity through standardized assays

  • Environmental conditions:

    • Control temperature, light exposure, and oxidative conditions

    • Consider the influence of pH and ionic strength on protein stability

    • Document all experimental conditions meticulously

How can I design experiments to compare psbZ function across different plant species?

To effectively compare psbZ function across different plant species, implement these design principles:

  • Comparative sequence analysis:

    • Align psbZ sequences from target species (e.g., Oenothera elata subsp. hookeri, Zygnema circumcarinatum, Magnolia tripetala)

    • Identify conserved and variable regions

    • Predict functional implications of sequence differences

  • Standardized functional assays:

    • Develop consistent protocols for measuring electron transport

    • Use identical experimental conditions for all species comparisons

    • Normalize data to account for species-specific differences in baseline activity

  • Heterologous expression systems:

    • Express psbZ variants from different species in the same expression system

    • Use consistent purification protocols to minimize methodology-induced variations

    • Tag proteins identically to ensure comparable detection and purification

  • Cross-species complementation:

    • Test ability of psbZ from one species to restore function in another species' deficient system

    • Quantify degree of functional restoration

    • Identify species-specific interaction requirements

  • Structural biology approaches:

    • Compare protein folding and stability across species variants

    • Assess membrane integration efficiency

    • Evaluate protein-protein interaction profiles

  • Statistical design considerations:

    • Use factorial experimental designs to test multiple species under various conditions

    • Implement appropriate statistical methods for multi-species comparisons

    • Control for phylogenetic relationships in data analysis

What are optimal techniques for expressing and purifying recombinant psbZ protein?

For optimal expression and purification of recombinant psbZ, researchers should consider these methodological approaches:

  • Expression systems:

    • E. coli is the predominant system for psbZ expression as evidenced in commercial preparations

    • Consider specialized E. coli strains designed for membrane protein expression

    • Codon optimization may improve expression efficiency

    • Alternative systems like yeast or insect cells may be considered for complex folding requirements

  • Expression conditions:

    • Optimize induction parameters (temperature, inducer concentration, timing)

    • Consider lower temperatures (16-25°C) to improve proper folding

    • Extended expression times may increase yield for difficult membrane proteins

    • Monitor growth curves to determine optimal harvest point

  • Fusion tags:

    • N-terminal His-tags are commonly used for psbZ purification

    • Consider the impact of tags on protein folding and function

    • Incorporate protease cleavage sites if tag removal is necessary

    • Evaluate tag accessibility in the folded protein

  • Membrane protein extraction:

    • Optimize cell lysis methods (sonication, pressure homogenization)

    • Select appropriate detergents for membrane solubilization

    • Consider native lipid co-extraction to maintain stability

    • Test various detergent:protein ratios

  • Purification strategy:

    • Implement initial capture via affinity chromatography (IMAC for His-tagged proteins)

    • Include secondary purification steps (ion exchange, size exclusion)

    • Monitor purity via SDS-PAGE (aim for >90% purity)

    • Consider on-column refolding for proteins in inclusion bodies

  • Quality assessment:

    • Verify identity via mass spectrometry or N-terminal sequencing

    • Assess oligomeric state via size exclusion chromatography

    • Confirm function through activity assays

    • Evaluate stability in final storage buffer

What analytical methods are most appropriate for studying psbZ structure and function?

Several complementary analytical methods are valuable for investigating psbZ structure and function:

  • Spectroscopic techniques:

    • Circular dichroism (CD) spectroscopy to assess secondary structure

    • Fluorescence spectroscopy to monitor protein folding and ligand binding

    • Absorption spectroscopy to measure chlorophyll interactions and electron transfer

    • EPR spectroscopy to track electron transport processes

  • Structural biology approaches:

    • X-ray crystallography for high-resolution structural determination (challenging for membrane proteins)

    • Cryo-electron microscopy for structure of psbZ within photosystem complexes

    • NMR spectroscopy for dynamics and interaction studies

    • Molecular modeling based on homologous structures

  • Biophysical characterization:

    • Differential scanning calorimetry (DSC) to measure thermal stability

    • Isothermal titration calorimetry (ITC) for binding energetics

    • Surface plasmon resonance (SPR) for interaction kinetics

    • Analytical ultracentrifugation for oligomeric state determination

  • Functional assays:

    • Oxygen evolution measurements to assess PSII activity

    • Chlorophyll fluorescence analysis for energy transfer efficiency

    • Electron transport assays using artificial electron acceptors

    • Time-resolved spectroscopy for electron transfer kinetics

  • Molecular biology techniques:

    • Site-directed mutagenesis to identify critical residues

    • Crosslinking studies to map protein-protein interactions

    • Proteoliposome reconstitution to study membrane behavior

    • In vivo complementation to verify functional activity

  • Advanced imaging:

    • Confocal microscopy for localization studies

    • FRET analysis for protein proximity measurements

    • Super-resolution microscopy for detailed structural organization

How should I design controls when studying the effects of environmental factors on psbZ function?

When investigating environmental influences on psbZ function, implement the following control strategies:

  • System validation controls:

    • Positive control: Known conditions that enhance psbZ function

    • Negative control: Conditions known to inhibit psbZ function

    • System control: Complete reaction system without environmental variable manipulation

  • Vehicle controls:

    • Include controls containing all solvents, buffers, or carriers used to introduce environmental factors

    • Match concentrations and volumes precisely between experimental and control groups

  • Control for confounding variables:

    • Control for light intensity when studying temperature effects

    • Account for pH changes when modifying salt concentrations

    • Monitor oxygen levels when adjusting CO2 concentration

    • Consider time-of-day effects when collecting sequential measurements

  • Statistical design considerations:

    • Use randomized complete block design to control for unwanted variation

    • Implement Latin square designs when multiple environmental factors are studied

    • Consider split-plot designs when some factors are difficult to randomize

  • Time-course controls:

    • Include time-matched controls for each experimental condition

    • Account for natural degradation of protein activity over time

    • Monitor system stability throughout experimental duration

  • Dose-response controls:

    • Test multiple levels of environmental factors

    • Include both sub-threshold and saturating conditions

    • Establish baseline responses before environmental manipulation

  • Species-specific controls:

    • When comparing across species, maintain identical environmental conditions

    • Consider evolutionary adaptations to specific environments when interpreting results

    • Account for natural habitat conditions of Oenothera elata (coastal, sandy soils, etc.)

What statistical approaches are appropriate for analyzing psbZ functional data?

When analyzing psbZ functional data, researchers should consider these statistical methodologies:

  • Descriptive statistics:

    • Calculate means, standard deviations, and coefficients of variation

    • Present data with appropriate error bars representing standard error or confidence intervals

    • Generate box plots or violin plots to visualize distribution characteristics

  • Inferential statistics:

    • Use t-tests for simple two-group comparisons

    • Implement ANOVA for multi-group comparisons, with appropriate post-hoc tests

    • Consider non-parametric alternatives (Mann-Whitney, Kruskal-Wallis) for non-normally distributed data

    • Apply correction for multiple comparisons (Bonferroni, Tukey, FDR) as appropriate

  • Regression analysis:

    • Linear regression for continuous relationships

    • Non-linear regression for complex dose-response curves

    • Multiple regression when analyzing effects of several independent variables

  • Experimental design-specific analysis:

    • Repeated measures ANOVA for within-subjects designs

    • Mixed models for nested designs or longitudinal data

    • Factorial ANOVA for multi-factor experiments

  • Advanced analytical approaches:

    • Principal component analysis (PCA) for dimension reduction

    • Cluster analysis for identifying patterns in complex datasets

    • Machine learning approaches for predictive modeling

    • Bayesian statistics for incorporating prior knowledge

  • Statistical power and sample size:

    • Calculate minimum sample sizes needed to detect effects of interest

    • Report effect sizes alongside p-values

    • Consider confidence intervals as alternatives to p-values

    • Acknowledge limitations of small sample sizes

How can I effectively integrate psbZ structural data with functional findings?

To successfully integrate structural and functional data about psbZ, implement these methodological approaches:

What approaches help distinguish direct effects of psbZ mutations from indirect photosystem impacts?

To differentiate direct effects of psbZ mutations from broader photosystem consequences, employ these methodological strategies:

  • Targeted mutagenesis design:

    • Create specific point mutations rather than deletions when possible

    • Target conserved vs. variable residues differentially

    • Create mutation series with gradually increasing severity

  • Hierarchical analysis:

    • Assess effects at increasing levels of complexity:

      • Isolated protein properties (folding, stability)

      • Direct interaction partners (binding affinity)

      • Subsystem function (electron transport rates)

      • Whole photosystem performance (photosynthetic efficiency)

  • Time-resolved analysis:

    • Monitor systems with sufficient temporal resolution to distinguish primary from secondary effects

    • Track the progression of perturbations through the system

    • Identify the timeline of compensatory responses

  • Complementation strategies:

    • Test whether wild-type protein restores function in mutant systems

    • Verify whether related proteins can substitute for mutated psbZ

    • Create chimeric proteins to map functional domains

  • Interaction network analysis:

    • Map the protein-protein interaction network around psbZ

    • Quantify changes in interaction strengths upon mutation

    • Trace effects through the network to identify direct vs. propagated impacts

  • Control system implementation:

    • Create parallel mutations in non-interacting portions of photosystem

    • Compare systems with equivalent destabilization but different mutation locations

    • Use in silico modeling to predict direct vs. indirect effects

  • Comparative genomics approach:

    • Analyze natural variations in psbZ across species

    • Correlate sequence differences with functional adaptations

    • Identify compensatory mutations that maintain function despite variation

How does psbZ from Oenothera elata subsp. hookeri compare evolutionarily to homologs in other photosynthetic organisms?

An evolutionary analysis of psbZ from Oenothera elata subsp. hookeri reveals important insights when compared to homologs from other photosynthetic organisms:

  • Sequence conservation patterns:

    • The core transmembrane regions show high conservation across species

    • Notable sequence differences exist between psbZ from Oenothera elata (MTIAFQLAVFALIATSSLLLISVPVVFASPEGWSSNKNVVFSGTSLWIGLVFLVGILNSL IS) and other species like Zygnema circumcarinatum (MTITFQLAVFALIVTSFLLVIGVPVVLASPDGWSSNKNTVFSGASLWIGLVFLVGILNSF VS)

    • N-terminal regions typically show higher variability than the core functional domains

    • Specific residues involved in cofactor binding remain highly conserved

  • Phylogenetic relationships:

    • psbZ shows distinct evolutionary patterns corresponding to major photosynthetic lineages

    • Oenothera's psbZ reflects its position within flowering plants (Angiosperms)

    • Comparison with green algae (e.g., Zygnema circumcarinatum) highlights divergence during land plant evolution

    • Molecular clock analysis suggests conservation of core function despite sequence divergence

  • Structural adaptations:

    • Species-specific variations often occur in regions interacting with other photosystem components

    • Adaptive changes correlate with environmental niches and photosynthetic strategies

    • Membrane integration sequences show adaptation to different thylakoid compositions

    • Subunit interface regions reflect co-evolution with partner proteins

  • Functional implications:

    • Despite sequence differences, core functional domains maintain electron transport capabilities

    • Species-specific variations may reflect adaptations to different light environments

    • Evening-flowering strategy of Oenothera may relate to specific photosystem adaptations

    • Stress response elements show greater divergence than core functional regions

  • Genomic context:

    • The psbZ gene (also known as ycf9) shows interesting evolutionary patterns in plastid genomes

    • Gene arrangement surrounding psbZ differs between species, with Oenothera showing unique inversions

    • The genomic region containing psbZ in Oenothera has undergone significant rearrangement compared to other flowering plants

    • These rearrangements have potentially disrupted transcriptional linkages, requiring adaptive changes

What experimental approaches would best elucidate the role of psbZ in stress adaptation?

To investigate psbZ's role in stress adaptation, implement these advanced experimental approaches:

  • Stress-specific experimental designs:

    • Expose systems to controlled stressors (high light, temperature extremes, drought)

    • Implement factorial designs to test interactions between multiple stressors

    • Compare wild-type and psbZ-modified systems under identical stress conditions

    • Track recovery kinetics following stress removal

  • Multi-omics integration:

    • Combine transcriptomics, proteomics, and metabolomics analyses

    • Track changes in psbZ expression, modification, and interaction patterns

    • Identify metabolic signatures associated with stress response

    • Use systems biology approaches to model stress response networks

  • Advanced imaging techniques:

    • Implement high-resolution chlorophyll fluorescence imaging

    • Use FRET-based sensors to track protein-protein interactions during stress

    • Apply super-resolution microscopy to visualize photosystem reorganization

    • Develop real-time imaging of reactive oxygen species production

  • Comparative ecophysiology:

    • Compare psbZ function in Oenothera populations from different habitats (coastal vs. inland)

    • Relate natural variation to habitat-specific stressors

    • Examine psbZ variation across the species' elevation gradient (sea level to 7,000 feet)

    • Correlate molecular adaptations with ecological performance

  • Genetic engineering approaches:

    • Create site-directed mutations targeting stress-responsive regions

    • Develop inducible expression systems for modified psbZ variants

    • Implement CRISPR-based gene editing for precise modification

    • Design chimeric proteins combining domains from stress-tolerant species

  • Advanced biophysical techniques:

    • Use electron paramagnetic resonance (EPR) to track stress-induced changes in redox state

    • Implement fast kinetic measurements to detect early stress responses

    • Apply pressure modulators to simulate water stress effects on protein function

    • Develop biosensors for real-time monitoring of photosystem status

  • Field-laboratory integration:

    • Design field experiments with controlled stress application

    • Collect samples across natural stress gradients

    • Implement rainout shelters, temperature manipulation, or light modification

    • Correlate laboratory findings with field performance

How might research on psbZ contribute to improving photosynthetic efficiency in agricultural applications?

Research on psbZ from Oenothera elata subsp. hookeri has several potential applications for improving agricultural photosynthetic efficiency:

  • Photosynthetic optimization strategies:

    • Identify psbZ variants with enhanced electron transport capacity

    • Engineer modifications that improve energy distribution between photosystems

    • Optimize the stability-flexibility balance for diverse environmental conditions

    • Develop crops with improved photosynthetic efficiency under fluctuating light

  • Stress tolerance enhancement:

    • Transfer stress-adaptive features from Oenothera's psbZ to crop species

    • Enhance recovery mechanisms following photoinhibition

    • Improve photoprotection without sacrificing photosynthetic capacity

    • Develop varieties with broader environmental tolerance

  • Biotechnological applications:

    • Use structure-function insights to design artificial photosynthetic systems

    • Develop biosensors based on psbZ interaction properties

    • Create synthetic biology platforms incorporating optimized photosystems

    • Engineer biofuel production systems with enhanced light harvesting

  • Resource use efficiency:

    • Improve water use efficiency through optimized photosynthetic performance

    • Enhance nitrogen utilization by reducing photosystem repair requirements

    • Optimize carbon fixation rates through improved electron transport

    • Reduce energy losses in the photosynthetic apparatus

  • Climate adaptation strategies:

    • Develop crops with photosystems optimized for predicted climate conditions

    • Enhance resilience to temperature extremes through modified electron transport

    • Improve recovery from drought-induced photosynthetic inhibition

    • Create varieties with adaptation potential to changing light environments

  • Methodological contributions:

    • Establish improved protocols for studying membrane protein function

    • Develop high-throughput screening methods for photosynthetic efficiency

    • Create standardized assays for evaluating photosystem performance

    • Design innovative experimental approaches for field-relevant testing

  • Translation to diverse crops:

    • Apply insights from Oenothera to major grain crops

    • Develop optimization strategies for both C3 and C4 photosynthesis

    • Create species-specific modification approaches based on comparative analysis

    • Identify universally applicable improvements versus species-specific adaptations

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