Difference between revisions of "Part:BBa K4390023"

Revision as of 15:27, 13 October 2022

Cellulose Binding Domain :: Gly-Ser Linker

This part is not compatible with BioBrick RFC10 assembly but is compatible with the iGEM Type IIS Part standard which is also accepted by iGEM.

Usage and Biology

The CBD is the non-catalytic domain of cellulase that recognises the beta-1,4-glycosidic linkage of cellulose and cellulose-derived polymers (e.g. carboxymethylcellulose). In the design, we used CenA for our CBD, the cellulose-binding domain of the cellulase endoglucanase A from Cellulomonas fimi (Din, N. et al., 1994). We attached the CBD to the N-terminus of the sfGFP via a glycine-serine linker.

This is an O part containing a cellulose-binding domain and a glycine-serine linker. The cellulose-binding domain allows for the expressed level 1 construct to bind to cellulose, while the glycine-serine linker introduces a short unstructured domain, minimising the risk of the cellulose-binding domain interfering with the activity of other parts. The 2022 Edinburgh-UHAS iGEM team used this part to add metallothioneins to a cellulose hydrogel.

Sequence and Features

Reference

Din, N., Forsythe, I., Burtnick, L., Gilkes, N., Miller, R., Warren, R. and Kilburn, D. (1994). The cellulose-binding domain of endoglucanase A (CenA) from Cellulomonas fimi: evidence for the involvement of tryptophan residues in binding. Molecular Microbiology, 11(4), pp.747-755.