Recombinant Morus indica ATP synthase subunit c, chloroplastic (atpH)

What is the structure and function of ATP synthase subunit c in chloroplasts?

ATP synthase subunit c forms the critical c-ring structure within the F0 sector of the ATP synthase complex. In chloroplasts, this transmembrane component creates a rotary motor driven by proton flow across the thylakoid membrane. The c-ring rotation mechanically couples to the F1 sector to catalyze ATP synthesis from ADP and inorganic phosphate.

In Morus indica, the chloroplastic ATP synthase subunit c (atpH) is an 81 amino acid protein with the sequence: MNPLISAASVIAAGLAVGLASIGPGVGQGTAAGQAVEGIARQPEAEGKIRGTLLLSLAFMEALTIYGLVVALALLFANPFV . This highly hydrophobic protein contains transmembrane domains that assemble into an oligomeric ring structure, with each c-subunit capable of binding and transporting one proton during rotation.

The protein functions as part of the ATP synthase complex, which serves as the main enzyme in the ATP biosynthetic pathway and photosynthesis . Its structure is critical for maintaining the proper proton-to-ATP ratio, which in plant chloroplasts is typically 4.6 (14 protons for 3 ATP molecules) .

How does recombinant Morus indica atpH protein differ from its native form?

The recombinant version of Morus indica ATP synthase subunit c is produced with an N-terminal His-tag in E. coli expression systems . This creates several key differences from the native protein:

• Additional N-terminal sequence: The His-tag adds approximately 6-10 histidine residues and potentially linker amino acids to the N-terminus of the protein.

• Altered solubility properties: The His-tag can change the protein's solubility characteristics, potentially making it more soluble in certain buffer conditions.

• Absence of post-translational modifications: Since E. coli lacks the chloroplastic post-translational machinery, any native modifications present in plant-derived atpH would be absent.

• Purification characteristics: The His-tag facilitates protein purification via metal affinity chromatography, allowing for isolation at ≥90% purity as determined by SDS-PAGE .

• Potential structural impacts: While the core function is preserved, the tag may slightly alter the protein's folding dynamics or oligomerization properties.

These differences must be considered when using the recombinant protein for structural or functional studies, as they may impact experimental outcomes.

What are the optimal storage and handling conditions for recombinant Morus indica atpH?

For optimal stability and activity maintenance of recombinant Morus indica atpH protein, researchers should follow these evidence-based protocols:

• Storage temperature: Store at -20°C/-80°C upon receipt. Long-term storage at -80°C is recommended for maintaining protein integrity beyond 6 months .

• Aliquoting strategy: Prepare multiple small-volume aliquots immediately after reconstitution to prevent repeated freeze-thaw cycles. Working aliquots can be stored at 4°C for up to one week .

• Reconstitution procedure:

  • Briefly centrifuge the vial prior to opening to collect contents

  • Reconstitute in deionized sterile water to 0.1-1.0 mg/mL

  • Add glycerol to a final concentration of 5-50% (optimally 50%)

• Buffer composition: The recombinant protein is supplied in Tris/PBS-based buffer with 6% Trehalose at pH 8.0 . This formulation stabilizes the protein during lyophilization and storage.

• Avoiding degradation factors: Minimize exposure to:

  • Repeated freeze-thaw cycles

  • Prolonged storage at room temperature

  • Extreme pH conditions

  • Proteases and oxidizing agents

Adhering to these storage guidelines ensures maximum protein stability and consistency in experimental results.

How can researchers assess the functional integrity of recombinant Morus indica atpH protein in experimental systems?

Comprehensive functional assessment of recombinant Morus indica atpH requires multiple complementary approaches:

• Proton translocation assays: Reconstitute the protein in liposomes containing pH-sensitive fluorescent dyes (e.g., ACMA or pyranine) to measure proton pumping activity across the membrane upon addition of an artificial proton gradient.

• ATP synthase activity reconstitution: Integrate the recombinant c-subunit with other ATP synthase components to assess if the c-ring forms properly and contributes to ATP synthesis. This requires:

  • Isolation of other ATP synthase subunits

  • Reconstitution in proteoliposomes

  • Measurement of ATP synthesis under proton gradient conditions

• Oligomerization assessment: Analyze c-ring formation using:

  • Blue native PAGE

  • Size exclusion chromatography

  • Electron microscopy techniques

• Binding studies: Validate functional attributes through:

  • Interaction measurements with other ATP synthase subunits

  • Proton binding/release kinetics using pH-jump techniques

  • Inhibitor binding studies (e.g., with oligomycin)

• Structural integrity analysis:

  • Circular dichroism spectroscopy to verify secondary structure

  • Limited proteolysis to assess proper folding

  • Thermal shift assays to determine stability

For comparative analysis, include control experiments with native chloroplast ATP synthase complexes isolated from Morus indica or related species to benchmark the recombinant protein performance against native standards.

What are the key considerations when designing experiments to study the role of atpH in plant stress responses?

When investigating atpH's role in plant stress responses, researchers should implement the following experimental design elements:

• Stress condition selection and standardization:

  • Define precise stress parameters (duration, intensity)

  • Apply multiple stress types (drought, salt, temperature) separately and in combination

  • Include recovery phases to assess reversibility

• Temporal expression profiling:

  • Monitor atpH expression at multiple timepoints (early, mid, late stress)

  • Correlate expression changes with physiological responses

  • Compare with known stress marker genes

• Tissue-specific analysis:

  • Compare atpH regulation in different plant tissues (leaves, roots)

  • Consider that ATP synthase upregulation occurs in stressed leaves of mulberry

  • Separately analyze young versus mature tissues

• Protein-level validation:

  • Perform western blotting to confirm proteomics results

  • Use appropriate antibodies against atpH or the His-tag

  • Include loading controls and quantification methods

• Functional correlation:

  • Measure ATP production rates under stress conditions

  • Assess proton gradient formation across thylakoid membranes

  • Correlate ATP synthase activity with photosynthetic efficiency

• Control experiments:

  • Include wild-type plants and appropriate negative controls

  • Compare with other ATP synthase subunits

  • Use plants with altered expression of atpH (if available)

Studies have shown that ATP synthase is upregulated in stressed mulberry leaves as confirmed by western blotting analysis, similar to observations in wheat and cucumber . This suggests that plants require increased energy production under stress conditions, making ATP synthase a critical component of stress response mechanisms.

How does the stoichiometry of the c-ring affect ATP synthesis efficiency, and what techniques can be used to investigate this?

The c-ring stoichiometry directly determines the ion-to-ATP ratio in ATP synthases, fundamentally influencing bioenergetic efficiency. Research approaches to investigate this relationship include:

• Manipulation of c-ring composition:

  • Site-directed mutagenesis of key residues affecting c-subunit packing

  • Heterologous expression of modified atpH genes

  • Construction of tobacco chloroplast mutants with altered c-ring stoichiometry (as demonstrated with 14 to 15 c-subunit increases)

• Biophysical characterization techniques:

  • Atomic force microscopy to directly visualize and count c-subunits

  • Cryo-electron microscopy for high-resolution structural analysis

  • Cross-linking mass spectrometry to determine subunit arrangement

• Functional consequences assessment:

  • Measure ATP/H⁺ ratios in isolated systems

  • Analyze proton flux requirements for ATP synthesis

  • Quantify ATP synthesis rates under varying pmf conditions

• Physiological impact analysis:

  • Monitor photosynthetic parameters (electron transport rates, NPQ)

  • Measure growth rates under different light conditions

  • Assess stress tolerance with altered ATP synthase stoichiometry

The research by Yamamoto et al. demonstrated that increasing the c-ring from 14 to 15 subunits in tobacco chloroplasts maintained normal growth despite reduced ATP synthase abundance (25% of wild-type levels) . This was achieved through enhancement of the membrane potential component of the proton motive force, ensuring sufficient proton flux without triggering low pH-induced feedback inhibition .

This table illustrates how c-ring modifications directly impact the fundamental bioenergetic parameters of ATP synthesis in chloroplasts.

What expression systems are optimal for producing functional recombinant Morus indica atpH protein?

Selecting the appropriate expression system for recombinant Morus indica atpH requires balancing multiple factors. Below are evidence-based methodological approaches with their respective advantages and challenges:

• E. coli expression systems (most common approach):

  • Methodology: The documented approach uses E. coli to express the full-length protein (1-81aa) with an N-terminal His-tag .

  • Advantages: High yield, simple culture conditions, rapid growth, well-established protocols.

  • Challenges: Membrane protein expression may lead to inclusion bodies, potential misfolding, lack of post-translational modifications.

  • Optimization strategies:

    • Use specialized E. coli strains (C41, C43) designed for membrane protein expression

    • Employ lower induction temperatures (16-20°C)

    • Add solubilizing agents or fusion partners to improve solubility

• Plant-based expression systems:

  • Methodology: Express in tobacco or other plant chloroplasts via chloroplast transformation.

  • Advantages: Native-like folding environment, appropriate post-translational processing, formation of proper membrane associations.

  • Challenges: Lower yields, slower production timeline, more complex purification.

  • Application: Particularly valuable for functional studies requiring authentic protein structure.

• Cell-free expression systems:

  • Methodology: Use wheat germ or E. coli extracts supplemented with lipids/detergents.

  • Advantages: Avoids toxicity issues, allows incorporation into nanodiscs or liposomes during synthesis.

  • Challenges: Higher cost, potential scalability limitations.

  • Best for: Initial screening or producing small amounts of highly pure protein.

For functional studies, the expression system should be selected based on the specific experimental requirements, with E. coli being suitable for structural studies and plant-based systems preferred when authentic function is critical.

What techniques are most effective for purifying and characterizing recombinant atpH protein?

A systematic multi-stage approach is required for effective purification and characterization of recombinant atpH:

• Purification workflow:

  • Initial extraction: Membrane solubilization using mild detergents (DDM, LDAO, or C12E8)

  • Primary purification: Immobilized metal affinity chromatography (IMAC) using the N-terminal His-tag

  • Secondary purification: Size exclusion chromatography to remove aggregates

  • Detergent exchange: Replacement with detergents suitable for downstream applications

• Purity assessment:

  • SDS-PAGE analysis: Standard for confirming >90% purity

  • Western blotting: Using antibodies against atpH or the His-tag

  • Mass spectrometry: For identity confirmation and detection of potential modifications

• Structural characterization:

  • Circular dichroism (CD): To assess secondary structure content

  • Dynamic light scattering: To evaluate size distribution and potential aggregation

  • Analytical ultracentrifugation: For oligomeric state determination

  • Cryo-electron microscopy: For high-resolution structural analysis of c-ring assembly

• Functional characterization:

  • Reconstitution into liposomes: For proton translocation studies

  • Patch-clamp experiments: To measure ion conductance

  • Assembly assays: To evaluate integration into larger ATP synthase complex

• Biophysical parameter determination:

  • Thermal stability: Using differential scanning calorimetry

  • Ligand binding: Using isothermal titration calorimetry

  • Conformational dynamics: Using hydrogen-deuterium exchange mass spectrometry

This methodological pipeline ensures thorough characterization from primary sequence verification to functional validation, providing a complete profile of the recombinant protein.

How can researchers effectively incorporate recombinant atpH into functional ATP synthase complexes for in vitro studies?

Reconstituting functional ATP synthase complexes containing recombinant atpH requires a strategic approach:

• Component preparation strategies:

  • Hybrid complex assembly: Combine recombinant atpH with isolated native components from chloroplasts

  • Full recombinant assembly: Express and purify all ATP synthase components individually

  • Partial complex reconstitution: Focus on F0 sector assembly to study proton translocation

• Reconstitution methodology:

  • Sequential addition protocol:

    1. Solubilize purified atpH in appropriate detergent

    2. Mix with other F0 components at optimal stoichiometric ratios

    3. Add F1 components under ATP/Mg²⁺ conditions

    4. Remove detergent using biobeads or dialysis

  • Co-expression approach: Express multiple components simultaneously in compatible systems

• Membrane incorporation techniques:

  • Proteoliposome formation:

    • Prepare liposomes with defined lipid composition

    • Add detergent-solubilized proteins

    • Remove detergent for spontaneous incorporation

  • Nanodisc assembly:

    • Incorporate protein into lipid bilayers surrounded by scaffold proteins

    • Provides defined membrane environment and size control

• Functional validation methods:

  • ATP synthesis assays:

    • Generate proton gradient using acid-base transition or light-driven systems

    • Measure ATP production using luciferase-based detection

  • Proton pumping measurements:

    • Monitor fluorescence changes of pH-sensitive dyes

    • Quantify proton:ATP stoichiometry under varying conditions

• Analytical approaches:

  • Single-molecule techniques: Observe rotational motion using attached fluorescent probes

  • Structural analysis: Verify complex integrity using negative-stain electron microscopy

  • Inhibitor studies: Confirm specificity using oligomycin and other known inhibitors

These methodological approaches enable detailed investigation of how the Morus indica atpH contributes to ATP synthase function, proton translocation mechanics, and energy coupling efficiency.

How is atpH expression and function altered during environmental stress in mulberry species?

The regulation of ATP synthase subunit c in mulberry species exhibits distinct patterns under environmental stress conditions:

These findings highlight the central role of ATP synthase regulation in plant energy homeostasis under stress conditions, making atpH an important target for understanding stress adaptation mechanisms in Morus species.

What is the relationship between atpH function and photosynthetic efficiency in plants?

The relationship between atpH function and photosynthetic efficiency is multifaceted and critically important for plant energy metabolism:

• Bioenergetic coupling parameters:

  • In plant chloroplasts with a c₁₄-ring, 14 H⁺ are required for one complete rotation of the c-ring

  • This rotation produces 3 molecules of ATP, resulting in an ion-to-ATP ratio of 4.67

  • Linear photosynthetic electron transport translocates 12 H⁺ across the thylakoid membrane per 2 NADPH produced

  • This generates an ATP/NADPH ratio of approximately 1.29, insufficient for Calvin-Benson cycle requirements

• ATP synthase and pmf regulation:

  • ATP synthase functions as a major consumer of proton motive force (pmf)

  • Its activity substantially affects the extent of photosynthetic downregulation

  • In plants with reduced ATP synthase levels, electron transport can be arrested due to enhanced photosynthetic control

• Light intensity adaptation mechanisms:

  • ATP synthase activity optimization balances ATP synthesis with downregulation of electron transport

  • This balance is crucial during fluctuating light conditions

  • The tradeoff is optimized by altering the ratio of ΔpH and Δψ components of pmf

• Engineering impacts on photosynthesis:

  • Manipulating c-ring stoichiometry affects the H⁺/ATP ratio and photosynthetic efficiency

  • In tobacco chloroplast mutants with increased c-ring size (14 to 15 subunits), plants maintained normal growth despite reduced ATP synthase abundance

  • This was achieved through enhancement of membrane potential contribution to pmf

These relationships demonstrate the complex interplay between ATP synthase function, photosynthetic electron transport, and plant energy metabolism, highlighting atpH's critical role in photosynthetic efficiency.

How does recombinant atpH protein research contribute to understanding the medicinal properties of Morus species?

Research on recombinant atpH protein provides valuable insights connecting energy metabolism to the medicinal properties of Morus species:

• Energy metabolism and diabetes connection:

  • Morus species demonstrate significant hypoglycemic effects beneficial for type 2 diabetes mellitus (DM2) treatment

  • ATP synthesis regulation is fundamentally linked to glucose metabolism through AMPK activation

  • Understanding atpH function helps elucidate how Morus extracts affect cellular energy sensing

• Mechanistic pathway interactions:

  • Mulberry extracts activate protein kinase by adenosine monophosphate (AMPK)

  • AMPK regulates glucose uptake and energetic homeostasis

  • AtpH research provides molecular-level understanding of how energy production interacts with these pathways

• Stress response and medicinal properties correlation:

  • AtpH upregulation occurs during plant stress

  • Many medicinal compounds in Morus are stress-responsive secondary metabolites

  • Understanding energy allocation during stress helps explain bioactive compound production

• Inflammation and energy metabolism:

  • Morus alba shows anti-inflammatory effects, reducing leukocyte migration

  • ATP metabolism is intrinsically linked to inflammatory processes

  • AtpH research connects energy production to inflammatory pathway regulation

• Translation to therapeutic applications:

  • Detailed understanding of atpH structure and function aids identification of bioactive compounds targeting energy metabolism

  • Recombinant protein studies facilitate screening of Morus-derived compounds that may modulate ATP synthase activity

  • This research bridges fundamental plant biochemistry with medicinal applications

The following table summarizes connections between atpH research insights and observed medicinal properties of Morus species:

This research area demonstrates how fundamental studies on chloroplast ATP synthase components can inform understanding of traditional medicinal plants' therapeutic properties.

How does the structure and function of atpH in Morus indica compare with other plant species?

Comparative analysis of ATP synthase subunit c across plant species reveals important insights about conservation and specialization:

The Morus indica atpH represents an important comparative model for understanding both the conserved aspects of ATP synthase function and the species-specific adaptations that contribute to unique physiological properties of mulberry trees.

What unique properties of Morus indica atpH have been identified through recombinant protein studies?

Recombinant protein studies have revealed several distinctive characteristics of Morus indica atpH that contribute to our understanding of this specific ATP synthase component:

• Structural features:

  • The 81-amino acid sequence of Morus indica atpH contains the characteristic hydrophobic regions required for membrane integration

  • The protein exhibits successful expression and folding when produced with an N-terminal His-tag in E. coli systems

  • The recombinant protein maintains >90% purity after purification, indicating stable structural properties

• Expression optimization:

  • Recombinant expression yields in E. coli are sufficient for structural and functional studies

  • The protein can be successfully recovered in lyophilized form and reconstituted for experimental use

  • This suggests favorable folding properties compared to some more challenging membrane proteins

• Stress-responsive regulation:

  • ATP synthase components in Morus species show specific upregulation patterns during stress response

  • This regulation appears to be part of the adaptation mechanism in mulberry trees

  • The pattern of expression changes provides insights into mulberry-specific energy management strategies

• Stability characteristics:

  • The recombinant protein shows stability in Tris/PBS-based buffer with 6% Trehalose at pH 8.0

  • Addition of 50% glycerol contributes to long-term stability

  • These properties facilitate experimental manipulation and functional studies

• Potential biotechnological applications:

  • The successful recombinant expression and purification of Morus indica atpH enables its use in:

    • Structural studies to understand mulberry-specific ATP synthase properties

    • Screening for compounds that may affect ATP synthesis in relation to Morus medicinal properties

    • Comparative studies with other plant species to identify specialized adaptations

These findings from recombinant protein studies provide a foundation for deeper investigation into the specific properties of ATP synthase in Morus indica and how they relate to the unique physiological and medicinal characteristics of mulberry trees.

How can evolutionary analysis of atpH sequences inform our understanding of ATP synthase adaptation across plant species?

Evolutionary analysis of atpH sequences provides valuable insights into ATP synthase adaptation and specialization:

• Phylogenetic analysis approaches:

  • Sequence alignment methodology:

    • Multiple sequence alignment of atpH from diverse plant species

    • Identification of conserved versus variable regions

    • Analysis of selection pressure across different domains

  • Tree construction techniques:

    • Maximum likelihood methods to infer evolutionary relationships

    • Bayesian approaches to estimate divergence times

    • Reconciliation with species trees to identify lineage-specific events

• Functional domain conservation:

  • Proton-binding site analysis:

    • Universal conservation of the essential glutamate residue

    • Varying conservation of surrounding residues affecting proton affinity

  • Interface residues:

    • Higher conservation in regions contacting other ATP synthase subunits

    • Variable regions potentially reflecting co-evolution with partner subunits

• Environmental adaptation signatures:

  • Climate correlation analysis:

    • Identification of sequence variations correlating with environmental conditions

    • Species from similar habitats showing convergent adaptations

  • Stress adaptation markers:

    • Variations in regulatory regions correlating with stress tolerance

    • Specific amino acid changes associated with thermal or drought adaptation

• C-ring stoichiometry evolution:

  • Residue packing determinants:

    • Identification of key residues determining c-subunit packing geometry

    • Correlation with known c-ring stoichiometries (13-15 subunits in plants)

  • Bioenergetic implications:

    • Analysis of how stoichiometry changes affect H⁺/ATP ratios

    • Adaptive significance of different ratios in various ecological contexts

• Methodological framework for comparative analysis:

This evolutionary perspective enables researchers to understand how ATP synthase has adapted to diverse environmental conditions across plant lineages, providing insights that can inform both basic science understanding and potential applications in crop improvement or biomimetic energy systems design.

What are the most promising future research directions for Morus indica atpH studies?

The study of recombinant Morus indica ATP synthase subunit c presents several compelling future research directions that could significantly advance our understanding of plant bioenergetics and stress adaptation:

• Structure-function relationship investigation:

  • High-resolution structural determination of the Morus indica c-ring

  • Comparative analysis with c-rings from other plant species

  • Investigation of how specific amino acid variations affect proton binding and translocation

• Stress adaptation mechanisms:

  • Detailed temporal analysis of atpH expression under various stress conditions

  • Investigation of post-translational modifications during stress response

  • Engineering of stress-responsive ATP synthase variants to improve plant resilience

• Integration with medicinal applications:

  • Exploration of connections between ATP synthase function and bioactive compound production

  • Screening of Morus-derived compounds for effects on ATP synthase activity

  • Development of ATP synthase-based assays for bioactive discovery

• Engineering for improved photosynthetic efficiency:

  • Modification of c-ring stoichiometry in crop plants based on insights from natural variation

  • Fine-tuning of H⁺/ATP ratios for specific agricultural conditions

  • Integration with other photosynthetic enhancement approaches

• Evolutionary bioenergetics:

  • Comprehensive phylogenetic analysis of atpH across plant lineages

  • Correlation of sequence variations with ecological adaptations

  • Ancestral sequence reconstruction to test evolutionary hypotheses

These research directions build upon the current understanding of Morus indica atpH while expanding into new frontiers that connect fundamental biophysics with applied aspects of plant biology, agriculture, and medicinal research.

What technical challenges remain in working with recombinant atpH and how might they be addressed?

Despite significant progress, several technical challenges persist in atpH research that require innovative approaches:

• Expression and purification optimization:

  • Challenge: Achieving high yields of properly folded membrane protein

  • Solutions:

    • Testing novel fusion partners to enhance solubility

    • Exploring cell-free expression systems with membrane mimetics

    • Developing improved detergent screening platforms

• Functional reconstitution barriers:

  • Challenge: Creating fully functional ATP synthase complexes with recombinant components

  • Solutions:

    • Developing co-expression systems for multiple subunits

    • Optimizing lipid compositions for proteoliposome formation

    • Utilizing nanodiscs or other membrane mimetics for stabilization

• Structural analysis limitations:

  • Challenge: Obtaining high-resolution structures of membrane-embedded c-rings

  • Solutions:

    • Applying advanced cryo-EM techniques optimized for membrane proteins

    • Using new detergents or amphipols that better preserve native structure

    • Developing improved crystallization approaches for membrane proteins

• In vivo relevance validation:

  • Challenge: Connecting in vitro findings to physiological roles in planta

  • Solutions:

    • Developing chloroplast transformation systems for Morus species

    • Creating plant expression systems with tagged versions for in vivo tracking

    • Using rapid transient expression systems for functional testing

• Biophysical measurement precision:

  • Challenge: Accurately measuring proton translocation and ATP synthesis in reconstituted systems

  • Solutions:

    • Implementing single-molecule techniques for direct observation

    • Developing more sensitive fluorescent probes for proton movement

    • Utilizing microfluidic approaches for precise control of conditions

Addressing these technical challenges will require interdisciplinary approaches combining advances in membrane protein biochemistry, structural biology techniques, and synthetic biology tools to fully exploit the potential of recombinant atpH for fundamental and applied research.

How can insights from Morus indica atpH research contribute to broader understanding of plant bioenergetics and stress adaptation?

Research on Morus indica atpH provides valuable insights that extend to broader plant science domains:

• Fundamental bioenergetic principles:

  • Understanding the molecular basis of proton-to-ATP energy conversion

  • Elucidating how plants balance energy production against photodamage risks

  • Revealing evolutionary solutions to the bioenergetic challenges of photosynthesis

• Stress adaptation frameworks:

  • Demonstrating how energy metabolism reconfiguration supports stress response

  • Identifying common patterns of ATP synthase regulation across stress types

  • Providing comparative context for how different plant lineages optimize energy use under stress

• Agricultural applications:

  • Informing approaches to engineer crops with improved photosynthetic efficiency

  • Identifying potential targets for enhancing stress tolerance in agriculture

  • Contributing to sustainable crop production under changing climate conditions

• Medicinal plant research integration:

  • Connecting traditional medicinal applications to molecular mechanisms

  • Bridging ethnobotanical knowledge with modern molecular understanding

  • Supporting evidence-based approaches to natural product research

• Evolutionary insights:

  • Revealing how fundamental energy conversion machinery adapts to diverse environments

  • Providing case studies in the evolution of multi-protein complexes

  • Demonstrating the balance between conservation and adaptation in essential cellular machinery

The specialized knowledge gained from Morus indica atpH research thus contributes to a comprehensive understanding of plant bioenergetics, with implications ranging from fundamental science to practical applications in agriculture, medicine, and biotechnology.