Surface-exposed positions in the transmembrane helices of the lactose permease of Escherichia coli determined by intermolecular thiol cross-linking

Proceedings of the National Academy of Sciences of the United States of America
Lan GuanH R Kaback

Abstract

Intermolecular thiol cross-linking was used to determine surface-exposed positions in 250 lactose permease mutants containing single-Cys replacements in each transmembrane helix. Significant cross-linking of monomers to produce homodimers is observed in nine mutants with a 5-A-long cross-linking agent containing bis-methane thiosulfonate reactive groups [position 78 (helix III); positions 185, 186, and 187 (helix VI); positions 263, 275, and 278 (helix VIII); and positions 308 (helix IX) and 398 (helix XII)]. The results are consistent with a current helix-packing model of the permease. Seven of the nine mutants that exhibit intermolecular cross-linking are located at or near the cytoplasmic ends of transmembrane helices; two are near periplasmic ends. The results suggest that only those Cys replacements accessible from the aqueous phase and not from the hydrophobic core of the membrane are susceptible to cross-linking because of the much higher reactivity of the thiolate anion relative to the thiol. Single-Cys mutants at positions 278 (helix VIII) and 398 (helix XII), which are located in opposite sides of the 12-helix bundle, exhibit similar rates of cross-linking with sigmoid kinetics. Furthermore, cross-linking is markedly ...Continue Reading

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Citations

Jun 14, 2005·Comptes rendus biologies·H Ronald Kaback
Sep 23, 2003·Journal of Molecular Biology·Eric R GeertsmaBert Poolman
Jul 18, 2012·Proceedings of the National Academy of Sciences of the United States of America·Yonggang ZhouH Ronald Kaback
Jul 7, 2011·The Journal of Biological Chemistry·Yonggang ZhouH Ronald Kaback
Jan 24, 2006·Journal of Bacteriology·Divya N AminMark S Johnson
May 13, 2006·Annual Review of Biophysics and Biomolecular Structure·Lan Guan, H Ronald Kaback
Jun 30, 2005·BMC Structural Biology·Oleg V KovalenkoMartin E Hemler
Oct 23, 2002·Proceedings of the National Academy of Sciences of the United States of America·Paul L SorgenMark E Girvin
Oct 21, 2003·Proceedings of the National Academy of Sciences of the United States of America·José Luis Vázquez-IbarH Ronald Kaback
May 16, 2002·Proceedings of the National Academy of Sciences of the United States of America·Lan GuanH Ronald Kaback
Sep 21, 2007·Proceedings of the National Academy of Sciences of the United States of America·Lan GuanH Ronald Kaback
Feb 1, 2006·Proceedings of the National Academy of Sciences of the United States of America·Lan GuanH Ronald Kaback
Aug 23, 2003·Proceedings of the National Academy of Sciences of the United States of America·Natalia ErmolovaH Ronald Kaback
Dec 19, 2006·Proceedings of the National Academy of Sciences of the United States of America·H Ronald KabackNatalia Ermolova
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May 3, 2019·Nature Communications·Yung-Ning ChangEric R Geertsma
Apr 22, 2015·Nature Communications·Kazuo TatebayashiHaruo Saito
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May 31, 2019·The Journal of General Physiology·H Ronald Kaback, Lan Guan
Dec 10, 2002·The Journal of Biological Chemistry·Lan GuanH Ronald Kaback
Jul 25, 2014·Archives of Biochemistry and Biophysics·Jennifer NeumannDirk Schneider
Oct 25, 2013·Biochemistry·Olga GaikoH Ronald Kaback

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