Key result
The TnphoA transposon successfully generated active alkaline phosphatase hybrid proteins when fused to secreted or complex cytoplasmic membrane proteins, providing a probe for protein export signals.
The development of the TnphoA transposon probe allows for the localization of export signals within proteins and the identification of new chromosomal genes for secreted and transmembrane proteins.
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May aid export signal mapping in bacteria; leaves open broader genomic applications pending validation.
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.
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Manoil et al. (1985) studied this question. TnphoA transposon was evaluated on Alkaline phosphatase activity of hybrid proteins. The TnphoA transposon successfully generated active alkaline phosphatase hybrid proteins when fused to secreted or complex cytoplasmic membrane proteins, providing a probe for protein export signals.
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