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PMID: 1856179 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

The malX malY operon of Escherichia coli encodes a novel enzyme II of the phosphotransferase system recognizing glucose and maltose and an enzyme abolishing the endogenous induction of the maltose system.

Journal of bacteriology ·Vol. 173 ·No. 15 ·1991-08-00 ·Pages 4862-76

Reidl J, Boos W

Abstract

Mutants lacking MalK, a subunit of the binding protein-dependent maltose-maltodextrin transport system, constitutively express the maltose genes. A second site mutation in malI abolishes the constitutive expression. The malI gene (at 36 min on the linkage map) codes for a typical repressor protein that is homologous to the Escherichia coli LacI, GalR, or CytR repressor (J. Reidl, K. Römisch, M. Ehrmann, and W. Boos, J. Bacteriol. 171:4888-4899, 1989). We now report that MalI regulates an adjacent and divergently oriented operon containing malX and malY. MalX encodes a protein with a molecular weight of 56,654, and the deduced amino acid sequence of MalX exhibits 34.9% identity to the enzyme II of the phosphototransferase system for glucose (ptsG) and 32.1% identity to the enzyme II for N-acetylglucosamine (nagE). When constitutively expressed, malX can complement a ptsG ptsM double mutant for growth on glucose. Also, a delta malE malT(Con) strain that is unable to grow on maltose due to its maltose transport defect becomes Mal+ after introduction of malI::Tn10 and the plasmid carrying malX. MalX-mediated transport of glucose and maltose is likely to occur by facilitated diffusion. We conclude that malX encodes a phosphotransferase system enzyme II that can recognize glucose and maltose as substrates even though these sugars may not represent the natural substrates of the system. The second gene in the operon, malY, encodes a protein of 43,500 daltons. Its deduced amino acid sequence exhibits weak homology to aminotransferase sequences. The presence of plasmid-encoded MalX alone was sufficient for complementing growth on glucose in a ptsM ptsG glk mutant, and the plasmid-encoded MalY alone was sufficient to abolish the constitutivity of the mal genes in a malK mutant. The overexpression of malY in a strain that is wild type with respect to the maltose genes strongly interferes with growth on maltose. This is not the case in a malT(Con) strain that expresses the mal genes constitutively. We conclude that malY encodes an enzyme that degrades the inducer of the maltose system or prevents its synthesis.

Related Genes
malX malY
MeSH Terms
Amino Acid Sequence Base Sequence Cloning, Molecular DNA, Bacterial/chemistry Down-Regulation Escherichia coli/enzymology,genetics,growth & development Genes, Bacterial/drug effects Glucose/genetics Maltose/biosynthesis,genetics Molecular Sequence Data Operon Phosphoenolpyruvate Sugar Phosphotransferase System/genetics,physiology Sequence Homology, Nucleic Acid Transaminases/genetics
Chemicals
DNA, Bacterial Maltose Transaminases Phosphoenolpyruvate Sugar Phosphotransferase System Glucose
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Reidl J
Department of Biology, University of Konstanz, Federal Republic of Germany.
Boos W
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Article Info
Journal
Journal of bacteriology
Abbr.
J Bacteriol
ISSN
0021-9193
DOI
10.1128/jb.173.15.4862-4876.1991
Published
1991-08-00
Pages
4862-76
Language
English
Region
United States
NLM ID
2985120R
PMCID
PMC208166
Subset
IM
Databases
GENBANK
M60722, M74478, M74479, M74480, M74481, M74482, M74483, M74484, S45931, S45951
External Links
PubMed source DOI: 10.1128/jb.173.15.4862-4876.1991 PMC Full Text View journal details
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