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  Role of pore-lining residues in defining the rate of water conduction by Aquaporin-0.

Saboe, P. O., Rapisarda, C., Kaptan, S., Hsiao, Y. S., Summers,. R., De Zorzi, R., et al. (2017). Role of pore-lining residues in defining the rate of water conduction by Aquaporin-0. Biophysical Journal, 112(5), 953-965. doi:10.1016/j.bpj.2017.01.026.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002C-E9AA-6 Version Permalink: http://hdl.handle.net/21.11116/0000-0001-4B59-8
Genre: Journal Article

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 Creators:
Saboe, P. O., Author
Rapisarda, C., Author
Kaptan, S.1, Author              
Hsiao, Y. S., Author
Summers, . R., Author
De Zorzi, R., Author
Dukovski, D., Author
Yu, J., Author
de Groot, B. L.1, Author              
Kumar, M., Author
Walz, T., Author
Affiliations:
1Research Group of Computational Biomolecular Dynamics, MPI for Biophysical Chemistry, Max Planck Society, ou_578573              

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 Abstract: Compared to other aquaporins (AQPs), lens-specific AQP0 is a poor water channel, and its permeability was reported to be pH-dependent. To date, most water conduction studies on AQP0 were performed on protein expressed in Xenopus oocytes, and the results may therefore also reflect effects introduced by the oocytes themselves. Experiments with purified AQP0 reconstituted into liposomes are challenging because the water permeability of AQP0 is only slightly higher than that of pure lipid bilayers. By reconstituting high amounts of AQP0 and using high concentrations of cholesterol to reduce the permeability of the lipid bilayer, we improved the signal-to-noise ratio of water permeability measurements on AQP0 proteoliposomes. Our measurements show that mutation of two pore-lining tyrosine residues, Tyr-23 and Tyr-149 in sheep AQP0, to the corresponding residues in the high-permeability water channel AQP1 have additive effects and together increase the water permeability of AQP0 40-fold to a level comparable to that of AQP1. Molecular dynamics simulations qualitatively support these experimental findings and suggest that mutation of Tyr-23 changes the pore profile at the gate formed by residue Arg-187.

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Language(s): eng - English
 Dates: 2017-03-142017-03-14
 Publication Status: Published in print
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 Rev. Method: Peer
 Identifiers: DOI: 10.1016/j.bpj.2017.01.026
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Title: Biophysical Journal
Source Genre: Journal
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Pages: - Volume / Issue: 112 (5) Sequence Number: - Start / End Page: 953 - 965 Identifier: -