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. 1988 May;170(5):2267–2275. doi: 10.1128/jb.170.5.2267-2275.1988

Export of hybrid proteins FhuA'-'LacZ and FhuA'-'PhoA to the cell envelope of Escherichia coli K-12.

J W Coulton 1, G K Reid 1, A Campana 1
PMCID: PMC211117  PMID: 3283107

Abstract

The fhuA gene of Escherichia coli K-12 encodes an outer membrane protein that acts as the ferrichrome-iron(III) receptor. To determine the export signals and sorting information within FhuA, gene fusions of fhuA'-'lacZ and fhuA'-'phoA were constructed. Although a FhuA'-'LacZ hybrid protein was detected in the Triton X-100-insoluble fraction of the cell envelope, direct immunoelectron microscopic observation showed that this protein remained in the cytoplasm. FhuA'-'PhoA hybrid proteins were all exported across the cytoplasmic membrane. Those hybrids containing up to 88 amino acids of FhuA (FhuA88) fused to PhoA were released along with other periplasmic proteins. Hybrids containing 180 or more amino acids of FhuA (FhuA180) fused to PhoA were associated with the outer membrane. It is proposed that some information inherent in the sequences between FhuA88 and FhuA180 confers stable association with the outer membrane.

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