Recombinant Kluyveromyces lactis ATP synthase subunit 9, mitochondrial (ATP9)

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Cat. No.

BT2037510

Source

in vitro E.coli expression system

Synonyms

ATP9; ATP synthase subunit 9, mitochondrial; Lipid-binding protein

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Description

Functional Insights from Recombinant ATP9

Assembly-Dependent Translation: Mutations in ATP9 disrupt ATP synthase assembly, triggering feedback loops to regulate translation rates of mtDNA-encoded subunits (e.g., ATP6, ATP8) .
Viability Studies: Deletion of ATP9 in K. lactis (via mtDNA rearrangement) is non-lethal, suggesting functional redundancy or compensation by nuclear genes .
Nuclear Relocation: Successful transfer of ATP9 to the nucleus in Saccharomyces cerevisiae demonstrated feasibility but revealed challenges in proper targeting and assembly .

Role in Proton Translocation and ATP Synthesis

ATP9’s decameric ring in F₀ facilitates proton translocation across the inner mitochondrial membrane. Rotation of this ring induces conformational changes in the F₁ domain, enabling ATP synthesis .

Genetic Regulation and Stoichiometry

Dual Genetic Origin: ATP9 (mtDNA) and ATP6 (mtDNA) are synthesized in mitochondria, while most ATP synthase subunits are nuclear-encoded. Feedback mechanisms ensure balanced production .
Feedback Loops: Assembly intermediates interact with ATP9 and ATP6 to regulate translation, preventing excess subunits that could dissipate membrane potential .

Experimental Models and Mutant Studies

Δatp9 Strains: Loss of ATP9 disrupts ATP synthase assembly and growth on non-fermentable substrates (e.g., glycerol). Suppression via mutations in F₁-ATPase (e.g., atp2.1) restores viability by altering ATP hydrolysis rates .
mtDNA Heteroplasmy: In Candida glabrata, mtDNA loss (e.g., Δatp6) is mitigated by nuclear ATP6 homologs, highlighting genetic plasticity in ATP synthase subunits .

Comparative Analysis of ATP9 in Fungi

Organism	ATP9 Gene Location	Functional Features	Key Findings
K. lactis	Mitochondrial DNA	Forms F₀ ring; not essential in Δatp9 mutants	Non-lethal mtDNA rearrangement deletes 22 C-terminal amino acids .
Erysiphe necator	Nuclear genome	Partially compensates for mtDNA atp9 loss	N-terminal domain loss correlates with defective ATP synthase .
S. cerevisiae	Nuclear (engineered)	Requires proper mitochondrial targeting	Nuclear ATP9 fails to restore ATP synthase function without mtDNA .

Product Specs

Form

Lyophilized powder
Please note: We prioritize shipping the format currently in stock. However, if you have specific format requirements, kindly include them in your order remarks, and we will accommodate your request.

Lead Time

Delivery time may vary depending on the purchase method or location. We recommend contacting your local distributors for specific delivery information.
All of our proteins are shipped with standard blue ice packs by default. If you require dry ice shipping, please contact us in advance as additional fees will apply.

Notes

Repeated freezing and thawing is not recommended. For optimal results, store working aliquots at 4°C for up to one week.

Reconstitution

We recommend briefly centrifuging the vial prior to 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. For long-term storage, we recommend adding 5-50% glycerol (final concentration) and aliquoting at -20°C/-80°C. Our standard final concentration of glycerol is 50%. Customers can use this as a reference.

Shelf Life

The shelf life is influenced by various factors, including storage conditions, buffer ingredients, temperature, and the intrinsic stability of the protein.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. For lyophilized form, the shelf life 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 will be determined during the production process. If you have a specific tag type requirement, please inform us, and we will prioritize developing the specified tag.

Synonyms

ATP9; ATP synthase subunit 9, mitochondrial; Lipid-binding protein

Buffer Before Lyophilization

Tris/PBS-based buffer, 6% Trehalose.

Datasheet

Please contact us to get it.

Expression Region

1-76

Protein Length

full length protein

Species

Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica)

Target Names

ATP9

Target Protein Sequence

MQLVLAAKYIGAGISTIGLLGAGIGIAIVFSALIQGVSRNPSLKDTLFPFAILGFALSEA TGLFCLMISFLLLYAV

Uniprot No.

P92811

Target Background

Function

Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) generates ATP from ADP in the presence of a proton gradient across the membrane, which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains: F(1), containing the extramembraneous catalytic core, and F(0), containing the membrane proton channel, linked by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain. A homomeric c-ring of probably 10 subunits is part of the complex rotary element.

Database Links

KEGG: kla:KllafMp01

Protein Families

ATPase C chain family

Subcellular Location

Mitochondrion membrane; Multi-pass membrane protein.

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Recombinant Kluyveromyces lactis ATP synthase subunit 9, mitochondrial (ATP9)

Description

Functional Insights from Recombinant ATP9

Role in Proton Translocation and ATP Synthesis

Genetic Regulation and Stoichiometry

Experimental Models and Mutant Studies

Comparative Analysis of ATP9 in Fungi

Product Specs

Target Background

Quick Inquiry

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