The Journal of General Physiology
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Published online Nov 27 2006. doi:10.1085/jgp.200609657
The Rockefeller University Press, 0022-1295 $8.00
JGP, Volume 128, Number 6, 721-729
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ARTICLE

 Secondary Structure of a KCNE Cytoplasmic Domain



Jessica M. Rocheleau, Steven D. Gage, and William R. Kobertz

Department of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, Worcester, MA 01605

Correspondence to William R. Kobertz: william.kobertz{at}umassmed.edu

Type I transmembrane KCNE peptides contain a conserved C-terminal cytoplasmic domain that abuts the transmembrane segment. In KCNE1, this region is required for modulation of KCNQ1 K+ channels to afford the slowly activating cardiac IKs current. We utilized alanine/leucine scanning to determine whether this region possesses any secondary structure and to identify the KCNE1 residues that face the KCNQ1 channel complex. Helical periodicity analysis of the mutation-induced perturbations in voltage activation and deactivation kinetics of KCNQ1-KCNE1 complexes defined that the KCNE1 C terminus is {alpha}-helical when split in half at a conserved proline residue. This helical rendering assigns all known long QT mutations in the KCNE1 C-terminal domain as protein facing. The identification of a secondary structure within the KCNE1 C-terminal domain provides a structural scaffold to map protein–protein interactions with the pore-forming KCNQ1 subunit as well as the cytoplasmic regulatory proteins anchored to KCNQ1–KCNE complexes.

Abbreviations used in this paper: {alpha}-PI, {alpha}-periodicity index; E1–E5, KCNE1–KCNE5; HA, hemagglutinin A; Q1, KCNQ1; TEVC, two-electrode voltage clamp; WT, wild-type.


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