PMID:3023349
| Citation |
Erni, B and Zanolari, B (1986) Glucose-permease of the bacterial phosphotransferase system. Gene cloning, overproduction, and amino acid sequence of enzyme IIGlc. J. Biol. Chem. 261:16398-403 |
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| Abstract |
The glucose-permease (IIGlc) of the bacterial phosphotransferase system mediates sugar transport across the cytoplasmic membrane concomitant with sugar phosphorylation. It also functions as a receptor for bacterial chemotaxis. The structural gene of the permease, ptsG, has been cloned on a multicopy plasmid, and transformants constitutively overproducing the protein 10-15 times over wild-type level have been isolated. Overproduction is slightly inhibited if transformants are grown in a glucose-containing medium. The complete amino acid sequence of the glucose-permease is deduced from the nucleotide sequence. It consists of 477 residues and is moderately hydrophobic. A comparison of the glucose-permease with the mannitol-permease (Lee, C. A., and Saier, M. H., Jr. (1983) J. Biol. Chem. 258, 10761-10767) does not reveal any obvious homology at the level of amino acid sequence. |
| Links | |
| Keywords |
Amino Acid Sequence; Base Sequence; Cloning, Molecular; DNA Restriction Enzymes; Escherichia coli/enzymology; Escherichia coli/genetics; Genes; Genes, Bacterial; Phosphoenolpyruvate Sugar Phosphotransferase System/genetics |
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