Difference between revisions of "Part:BBa K3016101"

Revision as of 11:00, 21 October 2019

Vibrio natriegens' aminotransferase Tat signal peptide

This part contains Vibrio natriegens' Aminotransferase Tat signal peptide. It is a twin-arginine (RR) motif containing signal peptide for periplasmic transport of proteins via the twin-arginine translocation (Tat) pathway. Derived from Vibrio natriegens’ Aminotransferase gene.

Biology

The twin-arginine translocation (Tat) pathway is capable of translocating fully folded proteins up to 150 kDa. It also contains a quality control feature of rejecting misfolded proteins. In some cases, disulfide bridge formation is not required for successful translocation. (Alanen et al., 2015)

Translocation using the tat-pathway requires the protein to contain a N-terminal signal peptide with a twin-arginine (RR) motif. The signal peptide is cleaved during the translocation process. A pair of V. natriegens’ native twin-arginine signal peptides identified by Aalto-Helsinki can be found here (TorAand Aminotransferase)

Use

This part can be N-terminally fused with your protein of choice to facilitate its periplasmic transport via the twin-arginine translocation (Tat) pathway.

Characterization

This part was only characterized by analysis of protein homology. For a more in-depth characterization of a Tat signal peptide in V. natriegens’, see TorA Sequence and Features

References:

Alanen, H. I., Walker, K. L., Suberbie, M. L. V., Matos, C. F., Bönisch, S., Freedman, R. B., ... & Robinson, C. (2015). Efficient export of human growth hormone, interferon α2b and antibody fragments to the periplasm by the Escherichia coli Tat pathway in the absence of prior disulfide bond formation. Biochimica et Biophysica Acta (BBA)-Molecular Cell Research, 1853(3), 756-763.