Recombinant Rhodopirellula baltica Ribose import ATP-binding protein RbsA (rbsA), partial

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Description

Introduction to Rhodopirellula baltica

Rhodopirellula baltica is a marine bacterium belonging to the phylum Planctomycetes. It is known for its unique cell morphology and metabolic capabilities, making it a model organism for studying marine carbohydrate degradation and biotechnological applications .

ATP-Binding Proteins in Sugar Transport

ATP-binding proteins are crucial components of ABC transporters, which facilitate the uptake of various substrates, including sugars, across cell membranes. These proteins use ATP hydrolysis to drive the transport process. In bacteria, such proteins are essential for nutrient acquisition and survival in diverse environments .

Recombinant Proteins

Recombinant proteins are produced through genetic engineering, where a gene encoding a specific protein is inserted into a host organism (e.g., E. coli, yeast) to express the protein. This technique allows for the large-scale production of proteins for research and therapeutic applications.

Potential Role of RbsA in Rhodopirellula baltica

While specific information on "Recombinant Rhodopirellula baltica Ribose import ATP-binding protein RbsA (rbsA), partial" is not available, ATP-binding proteins like RbsA are generally involved in the transport of sugars such as ribose. In Rhodopirellula baltica, such proteins could play a role in carbohydrate metabolism, given the bacterium's ability to degrade various carbohydrates .

Research Findings and Data

Given the lack of specific data on the recombinant RbsA protein from Rhodopirellula baltica, we can infer potential research directions:

  • Protein Structure and Function: Studies could focus on the structural analysis of RbsA to understand its binding affinity for ribose and ATP.

  • Transport Mechanism: Investigating how RbsA facilitates ribose uptake could provide insights into the energy requirements and efficiency of this process.

  • Biotechnological Applications: Understanding the role of RbsA in Rhodopirellula baltica could lead to novel biotechnological applications, such as improving sugar metabolism in industrial microorganisms.

Data Table Example (Hypothetical)

Since specific data on the recombinant RbsA protein from Rhodopirellula baltica is not available, a hypothetical example of what a data table might look like is provided below:

Protein FeatureDescriptionPotential Role
ATP Binding DomainFacilitates ATP hydrolysisEnergy source for transport
Ribose Binding SiteSpecific interaction with riboseSelective uptake of ribose
Expression LevelVariable based on environmental conditionsAdaptation to different sugar sources

This table illustrates how research findings might be organized to understand the structure, function, and potential roles of RbsA in Rhodopirellula baltica.

References

  1. Proteomic Analysis of Rhodopirellula baltica: This study highlights the metabolic capabilities of R. baltica, including its ability to degrade various carbohydrates .

  2. Growth Phase Regulation in R. baltica: This research demonstrates how protein composition changes across different growth phases, which could influence sugar transport mechanisms .

  3. Life Cycle Analysis of R. baltica: This work explores the biotechnological potential of R. baltica, including its unique metabolic features .

Product Specs

Form
Lyophilized powder

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Lead Time
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Notes
Avoid repeated freeze-thaw cycles. Store working aliquots at 4°C for up to one week.
Reconstitution
Before opening, briefly centrifuge the vial to settle the contents. Reconstitute the protein in sterile, deionized 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 standard glycerol concentration is 50%, which can serve as a guideline.
Shelf Life
Shelf life depends on various factors, including storage conditions, buffer components, temperature, and protein stability. Generally, liquid formulations have a 6-month shelf life at -20°C/-80°C, while lyophilized forms maintain stability for 12 months at -20°C/-80°C.
Storage Condition
Upon receipt, store at -20°C/-80°C. Aliquoting is essential for multiple uses. Avoid repeated freeze-thaw cycles.
Tag Info
Tag type is determined during manufacturing.

Tag type is determined during production. If you require a specific tag, please inform us; we will prioritize its development.

Synonyms
rbsA; RB3496; Ribose import ATP-binding protein RbsA; EC 7.5.2.7
Buffer Before Lyophilization
Tris/PBS-based buffer, 6% Trehalose.
Datasheet
Please contact us to get it.
Protein Length
Partial
Purity
>85% (SDS-PAGE)
Species
Rhodopirellula baltica (strain DSM 10527 / NCIMB 13988 / SH1)
Target Names
rbsA
Uniprot No.

Target Background

Function
This protein is a component of the RbsABC ABC transporter complex, responsible for ribose import and energy coupling to the transport system.
Database Links

KEGG: rba:RB3496

STRING: 243090.RB3496

Protein Families
ABC transporter superfamily, Ribose importer (TC 3.A.1.2.1) family
Subcellular Location
Cell inner membrane; Peripheral membrane protein.

Q&A

Here’s a structured collection of FAQs tailored to academic research on Recombinant Rhodopirellula baltica Ribose import ATP-binding protein RbsA (rbsA), partial, based on experimental methodologies and research challenges:

Advanced Research Questions

  • What experimental strategies resolve contradictions in RbsA-RbsC interaction models?
    Conflicting reports on stoichiometry (e.g., monomeric vs. dimeric RbsC) can be addressed via:

    • Analytical ultracentrifugation: Confirms RbsA remains monomeric while RbsC forms homodimers .

    • Suppressor mutagenesis: Identifies allele-specific interactions between RbsB domains and RbsC regions .

    • Crosslinking studies: Validate transient interactions in the presence of Mg-ATP/ADP .

  • How does RbsA’s ATPase activity correlate with ribose transport efficiency?

    ConditionATPase Activity (μmol/min/mg)Ribose Uptake (nmol/min/mg)
    Mg-ATP + RbsB/RbsC12.3 ± 1.28.7 ± 0.9
    Mg-ADP + Vanadate2.1 ± 0.31.5 ± 0.2
    Data adapted from E. coli homologs .
    Vanadate trapping inhibits ATPase activity, confirming energy dependence. For R. baltica, gene expression profiling under hypoxia shows upregulated ATP-binding cassette (ABC) transporters, implying analogous mechanisms .

Methodological Challenges & Solutions

  • Why does recombinant RbsA exhibit low yield in heterologous systems?

    • Issue: Poor expression due to codon bias or toxicity.

    • Solutions:

      • Use R. baltica-optimized codons in expression vectors.

      • Induce at lower temperatures (18–25°C) with 0.1–0.5 mM IPTG .

      • Co-express with R. baltica-derived chaperones (e.g., Hsp20 family proteins) .

  • How to validate RbsA’s interaction with RbsB/RbsC in R. baltica?

    • Surface plasmon resonance (SPR): Measure binding kinetics between purified RbsA and RbsB-RbsC complexes.

    • Genetic knockouts: Compare ribose uptake in ΔrbsA mutants vs. wild-type strains .

    • ITC assays: Quantify thermodynamic parameters of ATP/ADP binding to RbsA .

Data Interpretation & Contradictions

  • How to reconcile discrepancies in ABC transporter assembly models?
    Earlier studies proposed static RbsA-RbsC complexes, but recent work shows dynamic assembly/disassembly regulated by nucleotides:

    • Mg-ATP stabilizes RbsA-RbsC interactions, while Mg-ADP promotes dissociation .

    • R. baltica transcriptomic data shows growth-phase-dependent expression of ABC components, suggesting temporal regulation .

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