Molecular and General Genetics MGG

, Volume 181, Issue 4, pp 448–453 | Cite as

Regulation of methyl β-galactoside permease activity in pts and crr mutants of Salmonella typhimurium

  • Pieter W. Postma
  • Anja Schuitema
  • Chunglin Kwa


We have studied the regulation of the synthesis and activity of a major galactose transport system, that of methyl β-galactoside (MglP), in mutants of Salmonella typhimurium. Two classes of mutation that result in a (partially) defective phosphoenolpyruvate: sugar phosphotransferase system (PTS) interfere with MglP synthesis. pts mutations, which eliminate the general proteins of the PTS Enzyme I and/or HPr and crr mutations, which result in a defective glucose-specific factor IIIGle of the PTS, lead to a low MglP activity, as measured by methyl β-galactoside transport. In both ptsH,I, and crr mutants the amount of galactose binding protein, one of the components of MglP, is only 5%–20% of that in wild-type cells, as measured with a specific antibody. We conclude that synthesis of MglP is inhibited in pts and crr mutants. Once the transport system is synthesized, its transport activity is not sensitive to PTS sugars (i.e., no inducer exclusion occurs). The defect in pts and crr mutants with respect to MglP synthesis can be relieved in two ways: by externally added cyclic adenosine 3′, 5′-monophosphate (cAMP) or by a mutation in the cAMP binding protein. The conclusion that MglP synthesis is dependent on cAMP is supported by the finding that its synthesis is also defective in mutants that lack adenylate cyclase. pts and crr mutations do not affect growth of S. typhimurium on galactose, however, since the synthesis and activity of the other major galactose transport system, the galactose permease (GalP), is not sensitive to these mutations. If the galactose permease is eliminated by mutation, growth of pts and crr mutants on low concentrations of galactose becomes very slow due to inhibited MglP synthesis. Residual growth observed at high galactose concentrations is the result of yet another transport system with low affinity for galactose.


Galactose Adenylate Cyclase Phosphoenolpyruvate Phosphotransferase System Residual Growth 
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Copyright information

© Springer-Verlag 1981

Authors and Affiliations

  • Pieter W. Postma
    • 1
  • Anja Schuitema
    • 1
  • Chunglin Kwa
    • 1
  1. 1.Laboratory of Biochemistry, B.C.P. Jansen InstituteUniversity of AmsterdamAmsterdamThe Netherlands

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