| Types | DnaRegion
|
| Roles | Coding
CDS
|
| Sequences | BBa_K1869000_sequence (Version 1)
|
Description
The cyclopropane fatty acid (CFA) synthase is a cytosolic protein that reversibly associates with the membrane and catalyzes the addition of a methyl group. The methyl group is taken from S-adenosylmethionine (SAM) and attached to monounsaturated fatty acids (UFA) to generate CFAs. This part is useful in fortifying an organism's membrane. By expressing this protein, the phospholipid profile of the membrane changes to include these CFAs which decreases its permeability to small molecules, specifically weak acids. By decreasing its permeability, it is possible to increase the acid resistance of the cell to allow it to survive in more acidic conditions. This part is useful for creating organisms that are more tolerant of prolonged cultures or creating probiotics capable of surviving in the gut.
Notes
The CFA synthase sequence initially contained a PstI site, which was nulled using site-directed mutagenesis. We induced the mutation G318C to eliminate the cut site but ensure that it still codes for the same amino acid.
Source
The CFA synthase sequence was extracted, through PCR, from E. coli K-12 TG1. This protein is the primary protein in the CFA defense system found in E. coli, which is the single most impactful acid resistance system that it has.