Succinyl-CoA ligase [ADP-forming] subunit beta (SucC) is a mitochondrial metabolic enzyme that catalyzes the reversible conversion of succinyl-CoA to succinate in the tricarboxylic acid (TCA) cycle, coupled with ATP/ADP phosphorylation. In Yersinia pestis biovar Antiqua, this enzyme is encoded by the sucC gene (annotated as sucB in some bacterial systems). While its canonical role involves energy production, recent studies suggest non-metabolic functions in stress response and pathogen adaptation .
While sucC is primarily metabolic, studies in human homologs (SUCLA2) reveal redox regulation via stress granule assembly during cellular stress . Although direct evidence in Y. pestis is limited, analogous mechanisms may exist:
Oxidative Stress Mitigation: SUCLA2 in humans enhances catalase translation to combat reactive oxygen species (ROS) .
Anoikis Resistance: Mitochondrial-to-cytosolic translocation of SUCLA2 promotes cancer cell survival during detachment .
These findings imply that Y. pestis SucC could similarly support bacterial survival under host-induced stress (e.g., phagocytosis), though experimental validation is needed .
Analysis of Antiqua genomes reveals strain-specific adaptations:
| Function Lost | Antiqua | CO92 | KIM |
|---|---|---|---|
| TccC-family insecticidal toxin | Yes | No | Yes |
| Ail-like adhesin | Partial | No | Yes |
| RTX toxin transporter | No | Yes | Yes |
Antiqua retains metabolic genes like sucC but shows lineage-specific pseudogenization in virulence-associated loci (e.g., ail, yop effectors) .
Functional Characterization: No structural or enzymatic studies on purified SucC from Antiqua.
Metabolic vs. Virulence Roles: Unclear if sucC deletion impacts Y. pestis survival in hosts.
Structural Studies: Resolve SucC’s crystal structure to identify ATP/CoA-binding sites.
Gene Knockout Models: Assess ΔsucC strains for metabolic and virulence defects.
Stress Response Assays: Test SucC’s role under oxidative or nutrient-limited conditions.
KEGG: ypg:YpAngola_A1386