Nucleotide sequence of the iap gene, responsible for alkaline phosphatase isoenzyme conversion in Escherichia coli, and identification of the gene product

Y. Ishino, H. Shinagawa, K. Makino, M. Amemura, A. Nakatura

Research output: Contribution to journalArticle

675 Citations (Scopus)

Abstract

The iap gene in Escherichia coli is reponsible for the isozyme conversion of alkaline phosphatase. We analyzed the 1,644-nucleotide sequence of a chromosomal DNA segment that contained the iap gene and its flanking regions. The predicted iap product contained 345 amino acids with an estimated molecular weight of 37,919. The 24-amino-acid sequence at the amino terminus showed features characteristic of a signal peptide. Two proteins of different sizes were identified by the maxicell method, one corresponding to the Iap protein and the other corresponding to the processed product without the signal peptide. Neither the isozyme-converting activity nor labeled Iap proteins were detected in the osmotic-shock fluid of cells carrying a multicopy iap plasmid. The Iap protein seems to be asociated with the membrane.

Original languageEnglish
Pages (from-to)5429-5433
Number of pages5
JournalJournal of bacteriology
Volume169
Issue number12
DOIs
Publication statusPublished - Jan 1 1987

All Science Journal Classification (ASJC) codes

  • Microbiology
  • Molecular Biology

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