The Twin-arginine translocation (Tat) system is a Sec-independent protein transport pathway that enables the translocation of folded proteins across the cytoplasmic membrane in bacteria. In Rhodococcus erythropolis, the TatA protein is a critical component of this system, forming part of the translocase complex responsible for substrate recognition and membrane channel assembly . The recombinant "partial" TatA protein refers to a truncated form of this protein, often engineered for functional studies or biotechnological applications .
The Tat system in Rhodococcus spp. comprises three core proteins:
Transmembrane domain: Anchors TatA to the cytoplasmic membrane.
Cytoplasmic amphipathic helix: Facilitates oligomerization and pore formation .
Proton-motive force (PMF) dependence: TatA-mediated translocation is driven by PMF rather than ATP hydrolysis .
The TatA gene (tatA) is amplified via PCR and cloned into Rhodococcus-E. coli shuttle vectors (e.g., pTipQC2) .
Recombinant TatA is typically purified using nickel-affinity chromatography due to its hexahistidine tag .
The Tat system in Rhodococcus facilitates the secretion of lignin-modifying enzymes (e.g., peroxidases).
Recombinant TatA has been studied in R. erythropolis strains engineered for lignin valorization .
Channel activity: Organic solvent extracts of R. erythropolis cell walls containing TatA exhibit ion channel activity in lipid bilayers .
Oligomerization: TatA forms dynamic pores sized according to substrate dimensions .
| Feature | Tat System | Sec System |
|---|---|---|
| Substrate state | Folded proteins | Unfolded polypeptides |
| Energy source | Proton-motive force | ATP (via SecA) |
| Signal peptide | Twin-arginine motif (RRXFLK) | Hydrophobic α-helix |