Recombinant Cell division protein SepF 1 (sepF1)
Description
Introduction to Recombinant Cell Division Protein SepF
The Recombinant Cell division protein SepF, often referred to in the context of SepF rather than SepF1, plays a crucial role in bacterial cell division. It is particularly significant in Gram-positive and cyanobacteria, where it functions as a membrane anchor for the Z ring, a structure essential for cell division. This protein is involved in the polymerization of FtsZ, a tubulin homolog, into a ring-like structure at the midcell, which serves as a scaffold for other cell division proteins.
Structure and Function of SepF
SepF forms large protein rings with diameters of about 50 nm, as observed through electron microscopy . These rings are crucial for bundling FtsZ filaments and ensuring proper cell division. The protein's structure includes a globular domain at the C-terminal region, which is responsible for FtsZ binding, as revealed by yeast two-hybrid screens and crystal structure analyses . The N-terminal domain of SepF contains a membrane-binding site, allowing it to anchor the Z ring to the cell membrane .
Research Findings
Research on SepF has highlighted its importance in bacterial cell division, particularly in species lacking FtsA, another protein that typically anchors the Z ring. In such bacteria, SepF becomes essential for cell division to proceed correctly . Studies have shown that SepF mutants are unable to support growth in bacteria lacking FtsA, underscoring its critical role .
Data Table: Key Features of SepF
| Feature | Description |
|---|---|
| Protein Structure | Forms large protein rings; C-terminal globular domain for FtsZ binding; N-terminal membrane-binding domain. |
| Function | Anchors Z ring to cell membrane in bacteria lacking FtsA; essential for cell division in certain species. |
| Species Affected | Gram-positive and cyanobacteria. |
| Importance | Critical for proper cell division; becomes essential when FtsA is absent. |
Implications and Future Research
Understanding SepF's role in bacterial cell division has significant implications for microbiology and potential applications in biotechnology and medicine. Further research could explore how SepF interacts with other cell division proteins and its potential as a target for antimicrobial therapies.
References:
- Structural and genetic analyses reveal the protein SepF as a new membrane anchor for the Z ring in bacterial cell division.
- Structural and genetic analyses reveal the protein SepF as a new membrane anchor for the Z ring in bacterial cell division.
Product Specs
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Target Background
KEGG: sma:SAVERM_2329
STRING: 227882.SAV_2329
