Team:Groningen/Hydrophobins

From 2010.igem.org

Chaplins

Strongly hydrophobic proteins

In order to provide our Bacillus subtilis biofilm with hydrophobic properties we have turned to highly hydrophobic proteins originating from Streptomyces coelicolor, a soil dwelling bacterium which undergoes morphological differentiation as it goes through different stages in its life cycle, greatly resembling fungal growth. After submerged, vegetative growth aerial hyphae are formed which protrude from the moist substrate. The formation of these aerial hyphae appear to be highly dependent of strongly hydrophobic proteins called chaplins and have previously been described by Claessen et al (2003).

Two subgroups

Chaplins can roughly be categorized into two groups. The first group consists of chaplins A to C and are about 225 amino acids in size. These large chaplins contain two hydrophobic chaplin domains, a hydrophilic region and a cell wall anchor as well as a signaling sequence. The second group includes chaplin D to H and are with around 63 amino acids smaller than the afore mentioned chaplins. Being smaller, they only contain a hydrophobic chaplin domain and a signaling sequence.

Chaplins can roughly be categorized into two groups. The first group consists of chaplins A to C and are about 225 amino acids in size. These large chaplins contain two hydrophobic chaplin domains, a hydrophilic region and a cell wall anchor as well as a signaling sequence. The second group includes chaplin D to H and are with around 63 amino acids smaller than the afore mentioned chaplins. Being smaller, they only contain a hydrophobic chaplin domain and a signaling sequence.

Physical properties

Interestingly, purified chaplins can be used to hydrophillically coat normally hydrophobic surfaces such as the inside of eppendorf tubes. This is due to their amphipatic nature.

Chaplins are functional amyloids that will assemble by a catalytic process from monomers in polymer chain forming rod like structure surfaces called amyloid fibers. These fibers are very rigid and hard to break down. These fibers can only be broken when boiled in SDS. 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.

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