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Characterization of transmembrane segments 3, 4, and 5 of MalF by mutational analysis

Steinke, A., Grau, S., Davidson, A., Hofmann, E. and Ehrmann, Michael 2001. Characterization of transmembrane segments 3, 4, and 5 of MalF by mutational analysis. Journal of Bacteriology 183 (1) , pp. 375-381. 10.1128/JB.183.1.375-381.2001

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MalF and MalG are the cytoplasmic membrane components of the binding protein-dependent ATP binding cassette maltose transporter inEscherichia coli. They are thought to form the transport channel and are thus of critical importance for the mechanism of transport. To study the contributions of individual transmembrane segments of MalF, we isolated 27 point mutations in membrane-spanning segments 3, 4, and 5. These data complement a previous study, which described the mutagenesis of membrane-spanning segments 6, 7, and 8. While most of the isolated mutations appear to cause assembly defects, L323Q in helix 5 could interfere more directly with substrate specificity. The phenotypes and locations of the mutations are consistent with a previously postulated structural model of MalF.

Item Type: Article
Date Type: Publication
Status: Published
Schools: Biosciences
Publisher: American Society for Microbiology
ISSN: 0021-9193
Last Modified: 04 Jun 2017 06:39

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