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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Authors | T Nohno, T Saito, J S Hong |
Journal | Molecular & general genetics : MGG
(Mol Gen Genet)
Vol. 205
Issue 2
Pg. 260-9
(Nov 1986)
ISSN: 0026-8925 [Print] Germany |
PMID | 3027504
(Publication Type: Journal Article, Research Support, Non-U.S. Gov't, Research Support, U.S. Gov't, P.H.S.)
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Chemical References |
- Amino Acid Transport Systems, Basic
- Carrier Proteins
- Escherichia coli Proteins
- Membrane Proteins
- Membrane Transport Proteins
- glnP protein, E coli
- glutamine transport proteins
- glutamine permease
- DNA Restriction Enzymes
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Topics |
- 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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