Rhodopirellula baltica is a marine bacterium known for its unique cellular structures and metabolic capabilities . It belongs to the Planctomycetes-Verrucomicrobia-Chlamydiae (PVC) superphylum and possesses a number of interesting features, including the ability to respond to environmental changes .
Chaperonins are a class of proteins that assist in the proper folding of other proteins, preventing aggregation and ensuring correct functionality . They are essential for cell survival, particularly under stress conditions. GroL2 is a specific type of chaperonin, a 60 kDa protein found in R. baltica .
Recombinant GroL2, partial, is produced through genetic engineering techniques, where the gene encoding a portion of the GroL2 protein is inserted into a host organism (e.g., Escherichia coli) or baculovirus system . The host organism then produces the protein, which is subsequently isolated and purified. The term "partial" indicates that the produced protein is not the full-length GroL2 but a fragment of it.
Chaperonins like GroL2 are crucial for protein homeostasis within the cell. They are often upregulated under stress conditions, such as nutrient limitation, to maintain the correct folding of proteins and prevent aggregation .
R. baltica cells adapt metabolically to nutrient limitation by inducing chaperones .
Studying recombinant GroL2, partial, can provide insights into:
The structure and function of chaperonins.
Potential biotechnological applications, such as protein folding and drug discovery.
| Number of regulated genes | 62 h vs. 44 h | 82 h vs. 62 h | 96 h vs. 82 h | 240 h vs. 82 h |
|---|---|---|---|---|
| Total (%) * | 149 (2%) | 90 (1%) | 235 (3%) | 863 (12%) |
| Encoding hypothetical proteins (%) ** | 84 (56%) | 40 (44%) | 139 (59%) | 499 (58%) |
* (%) relative to the total number of 7325 open reading frames (ORFs) annotated in R. baltica genome.
** (%) relative to the total number of regulated genes.
KEGG: rba:RB8970
STRING: 243090.RB8970