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J. Biol. Chem., Vol. 265, Issue 36, 22554-22560, Dec, 1990
WM de Vos, I Boerrigter, RJ van Rooyen, B Reiche and W Hengstenberg
The plasmid-encoded lactose genes of the Lactococcus lactis
phosphotransferase system encoding Enzyme IIIlac (lacF) and Enzyme IIlac
(lacE) have been identified and cloned in Escherichia coli and L. lactis.
Nucleotide sequence and transcription analysis showed that these genes are
organized into a lactose-inducible operon with the gene order
lacF-lacE-lacG-lacX, the latter two genes encoding phospho-beta-
galactosidase and a 34-kDa protein with an unknown function, respectively.
The lac-operon is immediately followed by an IS element that is homologous
to ISS1. Enzyme IIIlac was purified from L. lactis and determination of its
NH2-terminal sequence demonstrated that the lacF gene starts with a TTG
codon and encodes a 105 amino acid protein (Mr = 11416). Cross-linking
studies with the purified enzyme showed that Enzyme IIIlac is active as a
trimer. A mutant lacF gene was identified in strain YP2-5 and appeared to
encode Enzyme IIIlac containing the missense mutation G18E. The lacF gene
could be expressed under control of vector-located promoter sequences
resulting in overproduction of Enzyme IIIlac in E. coli and complementation
of the L. lactis lacF mutant YP2-5. The deduced amino acid sequence of
Enzyme IIlac consists of 586 amino acids (Mr = 61562) and shows the
characteristics of a hydrophobic, integral membrane protein. The deduced
primary structures of the L. lactis Enzyme IIIlac and Enzyme IIlac are
homologous to those of Staphylococcus aureus (72 and 71% identity,
respectively) and Lactobacillus casei (48 and 47% identity, respectively).
In contrast, the organization of the lactose genes differs significantly
between those Gram-positive bacteria. Heterogramic homology in specific
domains was observed between the derived amino acid sequences of the
lactose-specific enzymes and that of E. coli Enzyme IIIcel and Enzyme
IIcel, which suggest a common function in the transport and phosphorylation
of these structurally related beta-glucosides.
Characterization of the lactose-specific enzymes of the phosphotransferase system in Lactococcus lactis
Department of Biophysical Chemistry, Netherlands Institute for Dairy Research (NIZO), Ede.
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