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Gene Review:

lacY - galactoside permease

Escherichia coli CFT073

El-Masry, E.M. et al., Dryselius, R. et al., Nie, Y. et al., Kaback, H.R. et al., Xie, J. et al., et al.

Klauda, Brooks,

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Disease relevance of lacY

An X-ray structure of the lactose permease of Escherichia coli (LacY) in an inward-facing conformation has been solved [1].

High impact information on lacY

In a functional lactose permease mutant from Escherichia coli (LacY) devoid of native Cys residues, almost every residue was replaced individually with Cys and tested for reactivity with the permeant alkylating agent N-ethylmaleimide in right-side-out membrane vesicles [2].
Energetics of Ligand-induced Conformational Flexibility in the Lactose Permease of Escherichia coli [3].
Phosphatidylethanolamine and monoglucosyldiacylglycerol are interchangeable in supporting topogenesis and function of the polytopic membrane protein lactose permease [4].
Sugar binding in lactose permease: anomeric state of a disaccharide influences binding structure [5].
This study was carried out to determine the effect of N,N-diethyl-m-toluamide (DEET) and pyridostigmine bromide (PB), alone and in combination, on P-gp expression using Escherichia coli leaky mutant transformed with Mdr1 gene (pT5-7/mdr1), which codes for P-gp or lactose permease (pT5-7/lacY) as negative control [6].

Biological context of lacY

Determination of lacZ and lacY mRNA levels revealed a pattern of reduction that was similar to the Lac-proteins, indicating a relation between translation inhibition and mRNA degradation as a response to antisense PNA treatment [7].

Analytical, diagnostic and therapeutic context of lacY

Isothermal titration calorimetry has been applied to characterize the thermodynamics of ligand binding to wild-type lactose permease (LacY) and a mutant (C154G) that strongly favors an inward facing conformation [3].

References

Lessons from lactose permease. Guan, L., Kaback, H.R. Annual review of biophysics and biomolecular structure. (2006) [Pubmed]
Site-directed alkylation and the alternating access model for LacY. Kaback, H.R., Dunten, R., Frillingos, S., Venkatesan, P., Kwaw, I., Zhang, W., Ermolova, N. Proc. Natl. Acad. Sci. U.S.A. (2007) [Pubmed]
Energetics of Ligand-induced Conformational Flexibility in the Lactose Permease of Escherichia coli. Nie, Y., Smirnova, I., Kasho, V., Kaback, H.R. J. Biol. Chem. (2006) [Pubmed]
Phosphatidylethanolamine and monoglucosyldiacylglycerol are interchangeable in supporting topogenesis and function of the polytopic membrane protein lactose permease. Xie, J., Bogdanov, M., Heacock, P., Dowhan, W. J. Biol. Chem. (2006) [Pubmed]
Sugar binding in lactose permease: anomeric state of a disaccharide influences binding structure. Klauda, J.B., Brooks, B.R. J. Mol. Biol. (2007) [Pubmed]
Interaction of pyridostigmine bromide and N,N-diethyl-m-toluamide alone and in combination with P-glycoprotein expressed in Escherichia coli leaky mutant. El-Masry, E.M., Abou-Donia, M.B. J. Toxicol. Environ. Health Part A (2006) [Pubmed]
Variable coordination of cotranscribed genes in Escherichia coli following antisense repression. Dryselius, R., Nikravesh, A., Kulyt??, A., Goh, S., Good, L. BMC Microbiol. (2006) [Pubmed]

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