PMID:3027504
| Citation |
Nohno, T, Saito, T and Hong, JS (1986) Cloning and complete nucleotide sequence of the Escherichia coli glutamine permease operon (glnHPQ). Mol. Gen. Genet. 205:260-9 |
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| Abstract |
The glutamine permease operon encoding the high-affinity transport system of glutamine in Escherichia coli could be cloned in one of the mini F plasmids, but not in pBR322 or pACYC184, by selection for restoration of the Gln+ phenotype, the ability to utilize glutamine as a sole carbon source. We determined the nucleotide sequence of the glutamine permease operon, which contains the structural gene of the periplasmic glutamine-binding protein (glnH), and indispensable component of the permease activity. The N-terminal amino acid sequence and the overall amino acid composition of the purified glutamine-binding protein were in good agreement with those predicted from the nucleotide sequence, if the N-terminal 22 amino acid residues were discounted. The latter comprised two Lys residues (nos. 2 and 6) followed by 16 hydrophobic amino acid residues and was assumed to be a signal peptide for transport into the periplasmic space. There were two additional reading frames (glnP and glnQ) downstream of glnH sharing a common promoter. It was concluded that the glnP and glnQ proteins as well as the glnH protein are essential for glutamine permease activity. |
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| Keywords |
Amino Acid Transport Systems, Basic; Base Sequence; Carrier Proteins/genetics; Cloning, Molecular; DNA Restriction Enzymes; Escherichia coli/genetics; Escherichia coli Proteins; Genes; Genes, Bacterial; Genotype; Membrane Proteins; Membrane Transport Proteins/genetics; Operon; Plasmids |
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