Recombinant Meyerozyma guilliermondii VMA21 is a synthetic version of the endoplasmic reticulum (ER)-resident protein critical for assembling the vacuolar-type H⁺-ATPase (V-ATPase). This enzyme facilitates proton transport across cellular membranes, essential for organelle acidification and cellular homeostasis. The recombinant form is produced via heterologous expression systems (e.g., E. coli, yeast, baculovirus, or mammalian cells) and is purified to ≥85% homogeneity, as determined by SDS-PAGE .
Gene ID: PGUG_02534
Organism: Meyerozyma guilliermondii (formerly Candida guilliermondii), a yeast-like fungus isolated from human infections, marine environments, and industrial products .
Protein Class: Integral membrane protein with a predicted role in V-ATPase assembly, analogous to yeast VMA21p .
In yeast, VMA21p interacts with V₀ subunits (e.g., proteolipid subunits and Vph1p) to mediate V₀ domain assembly in the ER . This process is critical for proton transport and lysosomal function. While Meyerozyma’s VMA21 has not been directly studied, its structural conservation implies analogous roles:
Chaperoning V₀ Subunits: Facilitating interactions between proteolipid rings and the 100-kDa V₀ subunit .
ER Export Coordination: Escorting assembled V₀ complexes to the Golgi for V₁ domain integration .
VMA21 mutations in humans cause X-linked myopathy with excessive autophagy (XMEA) . While Meyerozyma’s VMA21 is not directly implicated in human disease, its recombinant form could model V-ATPase-related pathologies.
Functional Validation: No studies confirm Meyerozyma VMA21’s role in V-ATPase assembly.
Interaction Mapping: Lack of data on binding partners (e.g., ATP6AP2 homologs).
Therapeutic Potential: Unexplored applications in antifungal drug development or biotechnology.
KEGG: pgu:PGUG_02534