L-Arabinose transport systems in Escherichia coli K-12

D. Kolodrubetz, R. Schleif

Research output: Contribution to journalArticle

25 Scopus citations

Abstract

Mutations in the arabinose transport operons of E. coli K-12 were isolated with the Mu lac phage by screening for cells in which β-galactosidase is induced in the presence of L-arabinose. Standard genetic techniques were then used to isolate numerous mutations in either of the two transport systems. Complementation tests revealed only one gene, araE, in the low-affinity arabinose uptake system. P1 transduction placed araE between lysA (60.9 min) and thyA (60.5 min) and closer to lysA. The operon of the high-affinity transport system was found to contain two genes: araF, which codes for the arabinose-binding protein, and a new gene, araG. The newly identified gene, araG, was shown by two-dimensional gel electrophoresis to encode a protein which is located in the membrane. Only defects in araG could abolish uptake by the high-affinity system under the conditions we used.

Original languageEnglish (US)
Pages (from-to)472-479
Number of pages8
JournalJournal of bacteriology
Volume148
Issue number2
StatePublished - 1981
Externally publishedYes

ASJC Scopus subject areas

  • Microbiology
  • Molecular Biology

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