TNPHOA - A TRANSPOSON PROBE FOR PROTEIN EXPORT SIGNALS
TNPHOA - A TRANSPOSON PROBE FOR PROTEIN EXPORT SIGNALS
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DOI：
10.1073/pnas.82.23.8129
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发表时间：
1985-01-01
影响因子：
11.1
通讯作者：
BECKWITH, J
中科院分区：
文献类型：
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作者：
MANOIL, C;BECKWITH, J
我们构建了转座子Tn5的衍生物，其允许产生由碱性磷酸酶（EC 3.1.3.1）组成的杂合蛋白，所述碱性磷酸酶缺乏与其他蛋白质的氨基末端序列融合的信号肽。如果与碱性磷酸酶融合的蛋白质提供促进输出的序列，从而补偿缺失的碱性磷酸酶信号肽，则这样的杂合体产生碱性磷酸酶活性。融合分泌的周质蛋白和复杂的细胞质膜蛋白导致碱性磷酸酶活性。TnphoA融合应该有助于定位蛋白质结构内的输出信号，例如跨膜蛋白，以及鉴定分泌和跨膜蛋白的新染色体基因。
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.