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Comparison of H5, S6, and H5-S6 exchanges on pore properties of voltage-dependent K+ channels. by M. Taglialatela; M.S. Champagne; J.A. Drewe; A.M. Brown is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

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Evidence is now substantial that membrane segments besides H, contribute to the pore of K+ channels. We found that substitution of the H, region of Shaker B (ShB) with the corresponding sequence of NGK2 expressed channels which retained the single channel K+ conductance (gK+) of the host ShB channel. A reverse chimera with ShB H, region transplanted into NGK2 also retained the gK+ of the host NGK2. Point mutations V443L+T449Y in ShB H, converted internal tetraethylammonium (TEA) affinity to NGK2 values, and T449Y converted external TEA affinity and Rb+ conductance (gRb+) to NGK2 values. In ShB, exchanging a short stretch of 9 amino acids located just past the transmembrane segment referred to as S,, post-S,, produced a large increase in gK+ with no effect on internal or external TEA blockade. Within S,, 3 important residues for internal TEA blockade were identified. Thus, H, determines external TEA blockade and both H, and S, may determine internal TEA blockade, but neither H, nor S, alone restored the donor gK+. However, chimeric channels in which HE, S,, and post-S, were exchanged transferred gK+ of NGK2 to ShB or the gK+ of ShB to NGK2. Thus, contributions from H,, S,, and its c

Who reads Comparison of H5, S6, and H5-S6 exchanges on pore properties of voltage-dependent K+ channels.?

Author

M. Taglialatela; M.S. Champagne; J.A. Drewe; A.M. Brown

Publisher

Elsevier BV

Published

1994

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)