期刊
JOURNAL OF BIOLOGICAL CHEMISTRY
卷 285, 期 16, 页码 12047-12054出版社
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M109.040360
关键词
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资金
- National Natural Science Foundation of China [30840028, 30970579, 30623005]
- Chinese Ministry of Science and Technology [2006AA02Z173]
- Basic Science and Advance Technology Research Program of Tianjin [08JCY-BJC25800]
- Ministry of Education of China [200800551035]
The voltage-gated proton channel Hv1 has a voltage sensor domain but lacks a pore domain. Although the C-terminal domain of Hv1 is known to be responsible for dimeric architecture of the channel, its role and structure are not known. We report that the full-length Hv1 is mainly localized in intracellular compartment membranes rather than the plasma membrane. Truncation of either the N or C terminus alone or both together revealed that the N-terminal deletion did not alter localization, but deletion of the C terminus either alone or together with the N terminus resulted in expression throughout the cell. These results indicate that the C terminus is essential for Hv1 localization but not the N terminus. In the 2.0 angstrom structure of the C-terminal domain, the two monomers form a dimer via a parallel C-helical coiled-coil, in which one chloride ion binds with the N eta atom of Arg(264). A pH-dependent structural change of the protein has been observed, but it remains a dimer irrespective of pH value.
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