NDLI: Functional interactions between putative intramembrane charged residues in the lactose permease of Escherichia coli.

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Functional interactions between putative intramembrane charged residues in the lactose permease of Escherichia coli.

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Functional interactions between putative intramembrane charged residues in the lactose permease of Escherichia coli.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Sahin-tóth, M. Dunten, R. L. Kaback, H. R. Gonzalez, A.
Description	Author Affiliation: Sahin-Tóth M ( Howard Hughes Medical Institute, Department of Physiology, University of California, Los Angeles 90024-1574.);
Abstract	Using a lactose permease mutant devoid of Cys residue ('C-less permease'), we systematically replaced putative intramembrane charged residues with Cys. Individual replacements for Asp-237, Asp-240, Glu-269, Arg-302, Lys-319, His-322, Glu-325, or Lys-358 abolish active lactose transport. When Asp-237 and Lys-358 are simultaneously replaced with Cys and/or Ala, however, high activity is observed. Therefore, when either Asp-237 or Lys-358 is replaced with a neutral residue, leaving an unpaired charge, the permease is inactivated, but neutral replacement of both residues yields active permease [King, S. C., Hansen, C. L. & Wilson, T. H. (1991) Biochim. Biophys. Acta 1062, 177-186]. Remarkably, moreover, when Asp-237 is interchanged with Lys-358, high activity is observed. The observations provide a strong indication that Asp-237 and Lys-358 interact to form a salt bridge. In addition, the data demonstrate that neither residue nor the salt bridge plays an important role in the transport mechanism. Thirteen additional double mutants were constructed in which a negative and a positively charged residue were replaced with Cys. Only Asp-240-->Cys/Lys-319-->Cys exhibits significant activity, accumulating lactose to 25-30% of the steady state observed with C-less permease. Replacing either Asp-240 or Lys-319 individually with Ala also inactivates the permease, but double mutants with neutral substitutions (Cys and/or Ala) at both positions exhibit essentially the same activity as Asp-240-->Cys/Lys-319-->Cys. In marked contrast to Asp-237 and Lys-358, interchanging Asp-240 and Lys-319 abolishes active lactose transport. The results demonstrate that Asp-240 and Lys-319, like Asp-237 and Lys-358, interact functionally and may form a salt bridge. However, the interaction between Asp-240 and Lys-319 is clearly more complex than the interaction between Asp-237 and Lys-358. In any event, the findings suggest that putative transmembrane helix VII lies next to helices X and XI in the tertiary structure of lactose permease.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	21
Volume Number	89
Language	English
Publisher	National Academy of Sciences
Publisher Date	1992-12-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Escherichia Coli Proteins Escherichia Coli Enzymology Membrane Transport Proteins Metabolism Monosaccharide Transport Proteins Symporters Amino Acid Sequence Biological Transport, Active Cell Membrane DNA, Bacterial Genetics Isolation & Purification Kinetics Chemistry Models, Structural Molecular Sequence Data Mutagenesis, Site-Directed Plasmids Protein Structure, Secondary Research Support, Non-U.S. Gov't Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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