POM34 is a non-essential transmembrane protein localized exclusively to the NPC in S. cerevisiae. Recombinant POM34 is typically expressed in E. coli with an N-terminal His tag for purification . Key characteristics include:
POM34 interacts with multiple nucleoporins (Nups) and contributes to NPC structural integrity:
Genetic Interactions: Synthetic lethality occurs in double mutants with nup170Δ, nup188Δ, nup59Δ, gle2Δ, nup159Δ, and nup82Δ . Functional complementation studies revealed allele-specific requirements for the N- or C-terminal regions in rescuing these mutants .
NPC Subcomplex: POM34 forms a transmembrane complex with Ndc1 and Pom152, which stabilizes NPC architecture . Disruption of this complex leads to pore dilation and nucleoporin mislocalization .
Role in Biogenesis: Depletion of POM34 in nup53Δ nup59Δ cells blocks new NPC assembly, causing cytoplasmic accumulation of newly synthesized Nup82 .
Recombinant POM34 is utilized in:
Antibody Production: Rabbit polyclonal antibodies against POM34 enable detection in Western blot (WB) and ELISA .
Interaction Studies: Affinity purification assays identify binding partners like Ndc1 and Pom152 .
Structural Analysis: Topology mapping and domain-deletion mutants clarify functional regions .
Functional Redundancy: POM34 and POM152 deletions are synthetically viable, but overexpression of Pom152 rescues pom34Δ nup170Δ and pom34Δ nup59Δ lethality .
Transport Defects: The pom34Δ nup188Δ mutant inhibits nuclear import via Kap104p and Kap121p pathways .
Evolutionary Conservation: POM34 homologs exist in fission yeast (Schizosaccharomyces pombe Mug31) , highlighting conserved NPC roles.
KEGG: sce:YLR018C
STRING: 4932.YLR018C