Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 279, Issue 7, Pages 5537-5548Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M310980200
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- NCI NIH HHS [CA 21765] Funding Source: Medline
- NIGMS NIH HHS [GM 34496] Funding Source: Medline
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2-O-alpha- Mannosyl- D- glycerate ( MGs) has been recognized as an osmolyte in hyperthermophilic but not mesophilic prokaryotes. We report that MG is taken up and utilized as sole carbon source by Escherichia coli K12, strainMC4100. Uptake is mediated by the P- enolpyruvate-dependent phosphotransferase system with the MG-inducible HrsA ( now called MngA) protein as its specific EIIABC complex. The apparent K-m of MG uptake in induced cells was 10 muM, and the V-max was 0.65 nmol/ min/ 10(9) cells. Inverted membrane vesicles harboring plasmid-encoded MngA phosphorylated MG in a P- enolpyruvate-dependent manner. A deletion mutant in mngA was devoid of MG transport but is complemented by a plasmid harboring mngA. Uptake of MG in MC4100 also caused induction of a regulon specifying the uptake and the metabolism of galactarate and glucarate controlled by the CdaR activator. The ybgG gene ( now called mngB) the gene immediately downstream of mngA encodes a protein with alpha- mannosidase activity. farR, the gene upstream of mngA ( now called mngR) had previously been characterized as a fatty acyl- responsive regulator; however, deletion of mngR resulted in the up- regulation of only two genes, mngA and mngB. The mngR deletion caused constitutive MG transport that became MG- inducible after transformation with plasmid expressed mngR. Thus, MngR is the regulator ( repressor) of the MG transport/ metabolism system. Thus, the mngR mngA mngB gene cluster encodes an MG utilizing system.
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