期刊
JOURNAL OF MOLECULAR BIOLOGY
卷 381, 期 3, 页码 569-580出版社
ACADEMIC PRESS LTD ELSEVIER SCIENCE LTD
DOI: 10.1016/j.jmb.2008.06.010
关键词
potassium channel; voltage-dependent gating; voltage sensor; membrane protein; electrical signaling
资金
- National Institutes of Health [GM43949]
- Cancer Research Foundation
- Howard Hughes Medical Institute
The gating of voltage-dependent potassium channels is controlled by conformational changes in voltage sensor domains. Previous studies have shown that the S1 and the S2 helices of the voltage sensor are static with respect to motion across the membrane, while the voltage sensor paddle consisting of the C-terminal half of S3 (S3b) and the charge-bearing S4 is mobile. The mobile component is attached to S1 and S2 via the S2-S3 turn and the N-terminal half of S3 (9a). In this study, we analyze KvAP, an archaebacterial voltage-dependent potassium channel, to study the mobility with respect to translation across the membrane of S3a. We utilize an assay based on attachment of tethered biotin and its site-specific accessibility to avidin. Our results reveal that the S3a helix does not move appreciably across the membrane in association with gating. The static behavior of S3a constrains the conformations available to the voltage sensor when it closes and suggests that a set of negative countercharges within the membrane's inner leaflet remains intact in the closed conformation. (C) 2008 Elsevier Ltd. All rights reserved.
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