Part:BBa_K305003
Hydrophobic protein chaplin E (chpE)
Strongly hydrophobic protein originating from Streptomyces coelicolor and codon optimized for Bacillus subtilis. It contains a hydrophobic chaplin domain and a signaling sequence.
Usage and Biology
The chaplins originate from Streptomyces coelicolor, which uses a variety of chaplins for the enforcement of its aerial hyphae.
There have to be found a variety of chaplains which can roughly be divided in two subcategories. The first is the group ranging from chaplin A till C. These are around 225 amino acids long and contain contain two hydrophobic chaplin domains, a hydrophilic region and a cell wall anchor as well as a signaling sequence. The second group of chaplins consist of chaplin D till H, which are approximately 63 amino acids long. These contain only one hydrophobic chaplin domain and a signaling sequence.
Chaplins can assemble into polymer chains, which form rod-like structures called amyloid fibers. These fibers are very rigid and hard to break down and can only be broken when boiled in SDS or with TCA and TFA treatment. They share distinguishing features with the medically important pathogenic amyloid fibers that are characteristic for many neurodegenerative diseases such as Alzheimer's, Huntington's, systemic amyloidosis and the prion diseases.
Physical properties
Interestingly, purified chaplins can be used to hydrophillically coat normally hydrophobic surfaces such as petri dishes. This is due to their amphipatic nature. This amphipatic property also gives them oil dispersing abilities.
Reference: Claessen, D; Rink, R; de Jong, W et al. 2003. A novel class of secreted hydrophobic proteins is involved in aerial hyphae formation in Streptomyces coelicolor by forming amyloid-like fibrils. Genes Dev 17 1714-1726
Part Characterization
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000COMPATIBLE WITH RFC[1000]
| None |