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KMID : 0545119990090050582
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Journal of Microbiology and Biotechnology
1999 Volume.9 No. 5 p.582 ~ p.588
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Cloning,Nucleotide Sequencing, and Characterization of the ptsG Gene Encoding Glucose-Specific Enzyme II of the Phosphotransferase System from Brevibacterium lactofermentum
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Yoon, Ki Hong
Lee, Kyu Nam/Lee, Jung Kee/Park, Se Cheol
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Abstract
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A Brevibacterium lactofermentum gene coding for a glucose-specific permease of the phosphoenolpyruvate-dependent phosphotransferase system (PTS) was cloned, by complementing an Escherichia coli mutation affecting a ptsG gene with the B. lactofermentum genomic library, and completely sequenced. The gene was identified as a ptsG, which enables an E. coli transformant to transport non-metabolizable glucose analogue 2-deoxyglucose (2DG). The ptsG gene of B. lactofermentum consists of an open reading frame of 2,025 nucleotides encoding a polypeptide of 674 amino acid residues and a TAA stop codon. The 3´ flanking region contains two stem-loop structures which may be involved in transcriptional termination. The deduced amino acid sequence of the B. lactofermentum enzyme Ⅱ^Glc specific to glucose (EIIG^Glc) has a high homology with the Corynebacterium glutamicum enzyme Ⅱ^man specific to glucose and mannose (EII^man), and the Brevibacterium ammonia genes enzyme Ⅱ^Glc specific to glucose (EII^Glc). The 171-amino-acid C-terminal sequence of the EII^Glc is also similar to the Escherichia coli enzyme IIA^Glc specific to glucose (IIA^Glc). It is interesting that the arrangement of the structural domains, IIBCA, of the B. lactofermentum EII^Glc protein is identical to that of EIIs specific to sucrose or β- glucoside. Several in vivo complementation studies indicated that the B. lactofermentum EII^Glc protein could replace both EII^Glc and EIIA^Glc in an E. coli ptsG mutant or crr mutant, respectively.
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