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. 1981 Nov;148(2):472–479. doi: 10.1128/jb.148.2.472-479.1981

L-arabinose transport systems in Escherichia coli K-12.

D Kolodrubetz, R Schleif
PMCID: PMC216229  PMID: 7028715

Abstract

Mutations in the arabinose transport operons of Escherichia coli K-12 were isolated with the Mu lac phage by screening for cells in which beta-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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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