Probing the Dynamics and Structural Topology of the Reconstituted Human KCNQ1 Voltage Sensor Domain (Q1-VSD) in Lipid Bilayers Using Electron Paramagnetic Resonance Spectroscopy.
Journal
Biochemistry
ISSN: 1520-4995
Titre abrégé: Biochemistry
Pays: United States
ID NLM: 0370623
Informations de publication
Date de publication:
19 02 2019
19 02 2019
Historique:
pubmed:
9
1
2019
medline:
27
11
2019
entrez:
9
1
2019
Statut:
ppublish
Résumé
KCNQ1 (Kv7.1 or KvLQT1) is a potassium ion channel protein found in the heart, ear, and other tissues. In complex with the KCNE1 accessory protein, it plays a role during the repolarization phase of the cardiac action potential. Mutations in the channel have been associated with several diseases, including congenital deafness and long QT syndrome. Nuclear magnetic resonance (NMR) structural studies in detergent micelles and a cryo-electron microscopy structure of KCNQ1 from Xenopus laevis have shown that the voltage sensor domain (Q1-VSD) of the channel has four transmembrane helices, S1-S4, being overall structurally similar with other VSDs. In this study, we describe a reliable method for the reconstitution of Q1-VSD into (POPC/POPG) lipid bilayer vesicles. Site-directed spin labeling electron paramagnetic resonance spectroscopy was used to probe the structural dynamics and topology of several residues of Q1-VSD in POPC/POPG lipid bilayer vesicles. Several mutants were probed to determine their location and corresponding immersion depth (in angstroms) with respect to the membrane. The dynamics of the bilayer vesicles upon incorporation of Q1-VSD were studied using
Identifiants
pubmed: 30620191
doi: 10.1021/acs.biochem.8b01042
pmc: PMC6456808
mid: NIHMS1018491
doi:
Substances chimiques
KCNQ1 Potassium Channel
0
KCNQ1 protein, human
0
Lipid Bilayers
0
Phosphatidylcholines
0
Phosphatidylglycerols
0
Spin Labels
0
1-palmitoyl-2-oleoylglycero-3-phosphoglycerol
81490-05-3
1-palmitoyl-2-oleoylphosphatidylcholine
TE895536Y5
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, Non-P.H.S.
Langues
eng
Sous-ensembles de citation
IM
Pagination
965-973Subventions
Organisme : NHLBI NIH HHS
ID : R01 HL122010
Pays : United States
Organisme : NIGMS NIH HHS
ID : R35 GM126935
Pays : United States
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