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Sugar recognition by CscB and LacY.

Junichi Sugihara¹, Irina Smirnova, Vladimir Kasho

¹Department of Physiology, University of California Los Angeles, Los Angeles, California 90095-7327, United States.

|November 24, 2011

Summary

Escherichia coli permeases CscB and LacY transport sugars. CscB recognizes the fructofuranosyl moiety, while LacY specifically binds the galactopyranosyl moiety, revealing distinct substrate specificities.

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Area of Science:

Biochemistry
Molecular Biology
Microbiology

Background:

Sucrose permease (CscB) and lactose permease (LacY) from Escherichia coli are H(+) symporters in the major facilitator superfamily.
Both proteins facilitate sugar transport across the cytoplasmic membrane, but have distinct known substrates: CscB for sucrose and LacY for galactopyranosides.

Purpose of the Study:

To investigate the substrate specificity determinants of CscB and LacY.
To compare the binding characteristics of CscB and LacY using various sugar substrates.

Main Methods:

Transport assays using Escherichia coli cells overexpressing CscB or LacY.
Testing of various sugars including sucrose, fructose, lactulose, and different pyranosides and furanosides.

Main Results:

CscB transported sucrose, fructose, and lactulose, but not glucopyranosides, indicating low specificity for the glucopyranosyl moiety.
Inhibition studies suggested the C(3)-OH group of the fructofuranosyl ring is important for CscB recognition.
LacY efficiently transported lactulose, with specificity directed towards the galactopyranosyl moiety, similar to lactose.

Conclusions:

CscB's substrate specificity is primarily determined by the fructofuranosyl moiety.
LacY's substrate specificity is primarily determined by the galactopyranosyl moiety.
These findings highlight distinct molecular recognition mechanisms for sugar transport in homologous permeases.