Gloeobacter violaceus PCC 7421 has a 4.66 Mbp circular chromosome with 4,430 protein-coding genes, including a single rRNA operon and 45 tRNA genes . The rpsP gene is part of this operon, likely co-transcribed with other ribosomal proteins.
Comparative genomics with Gloeobacter kilaueensis and Gloeobacter morelensis highlights:
Low ANI (92.6%) between G. violaceus and G. morelensis, despite near-identical 16S rRNA sequences .
Core gene clusters shared among Gloeobacter species include ribosomal proteins, underscoring their conserved roles .
Recombinant rpsP is expressed in heterologous hosts (e.g., E. coli) and purified via affinity chromatography. The protein is stable in Tris-based buffers with 50% glycerol and retains functionality for downstream assays .
While direct studies on Gloeobacter rpsP are sparse, homologous bacterial proteins (e.g., E. coli rpsA) highlight roles in:
Autogenous regulation: Competing with mRNA for ribosomal protein binding to control translation .
Stress response: Modulating ribosome activity during heat shock or nutrient deprivation .
The recombinant protein serves as a reference standard in:
Antibody validation for WB and ELISA.
Protein interaction studies involving 16S rRNA or assembly factors.
Mechanistic Studies: Investigate rpsP’s role in Gloeobacter ribosome biogenesis and stress response.
Evolutionary Biology: Compare rpsP across Gloeobacter species to map functional divergence.
Biotechnological Exploitation: Explore applications in synthetic biology or antibiotic resistance studies.