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 language | English (US) |
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Pages (from-to) | 472-479 |
Number of pages | 8 |
Journal | Journal of bacteriology |
Volume | 148 |
Issue number | 2 |
State | Published - 1981 |
Externally published | Yes |
ASJC Scopus subject areas
- Microbiology
- Molecular Biology