Crossref journal-article
Proceedings of the National Academy of Sciences
Proceedings of the National Academy of Sciences (341)
Abstract

We constructed a derivative of transposon Tn5 that permits the generation of hybrid proteins composed of alkaline phosphatase (EC 3.1.3.1) lacking its signal peptide fused to amino-terminal sequences of other proteins. Such a hybrid gives alkaline phosphatase activity if the protein fused to alkaline phosphatase contributes sequences that promote export and thus compensate for the missing alkaline phosphatase signal peptide. Fusions to both a secreted periplasmic protein and a complex cytoplasmic membrane protein led to alkaline phosphatase activity. TnphoA fusions should help localize export signals within the structure of a protein, such as a transmembrane protein, as well as identify new chromosomal genes for secreted and transmembrane proteins.

Bibliography

Manoil, C., & Beckwith, J. (1985). TnphoA: a transposon probe for protein export signals. Proceedings of the National Academy of Sciences, 82(23), 8129–8133.

Authors 2
  1. C Manoil (first)
  2. J Beckwith (additional)
References 0 Referenced 805

None

Dates
Type When
Created 19 years, 2 months ago (May 31, 2006, 5:50 a.m.)
Deposited 3 years, 4 months ago (April 13, 2022, 12:09 p.m.)
Indexed 4 months, 2 weeks ago (April 8, 2025, 5:39 p.m.)
Issued 39 years, 8 months ago (Dec. 1, 1985)
Published 39 years, 8 months ago (Dec. 1, 1985)
Published Online 39 years, 8 months ago (Dec. 1, 1985)
Published Print 39 years, 8 months ago (Dec. 1, 1985)
Funders 0

None

@article{Manoil_1985, title={TnphoA: a transposon probe for protein export signals.}, volume={82}, ISSN={1091-6490}, url={http://dx.doi.org/10.1073/pnas.82.23.8129}, DOI={10.1073/pnas.82.23.8129}, number={23}, journal={Proceedings of the National Academy of Sciences}, publisher={Proceedings of the National Academy of Sciences}, author={Manoil, C and Beckwith, J}, year={1985}, month=dec, pages={8129–8133} }