A native prokaryotic voltage-dependent calcium channel with a novel selectivity filter sequence
Voltage-dependent Ca2+ channels (Cavs) are indispensable for coupling action potentials with Ca2+ signaling in living organisms. The structure of Cavs is similar to that of voltage-dependent Na+ channels (Navs). It is known that prokaryotic Navs can obtain Ca2+ selectivity by negative charge mutatio...
| Main Authors: | , , , , , |
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| Format: | Article |
| Language: | English |
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eLife Sciences Publications Ltd
2020-02-01
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| Series: | eLife |
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| Online Access: | https://elifesciences.org/articles/52828 |
| _version_ | 1811180508431777792 |
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| author | Takushi Shimomura Yoshiki Yonekawa Hitoshi Nagura Michihiro Tateyama Yoshinori Fujiyoshi Katsumasa Irie |
| author_facet | Takushi Shimomura Yoshiki Yonekawa Hitoshi Nagura Michihiro Tateyama Yoshinori Fujiyoshi Katsumasa Irie |
| author_sort | Takushi Shimomura |
| collection | DOAJ |
| description | Voltage-dependent Ca2+ channels (Cavs) are indispensable for coupling action potentials with Ca2+ signaling in living organisms. The structure of Cavs is similar to that of voltage-dependent Na+ channels (Navs). It is known that prokaryotic Navs can obtain Ca2+ selectivity by negative charge mutations of the selectivity filter, but native prokaryotic Cavs had not yet been identified. We report the first identification of a native prokaryotic Cav, CavMr, whose selectivity filter contains a smaller number of negatively charged residues than that of artificial prokaryotic Cavs. A relative mutant whose selectivity filter was replaced with that of CavMr exhibits high Ca2+ selectivity. Mutational analyses revealed that the glycine residue of the CavMr selectivity filter is a determinant for Ca2+ selectivity. This glycine residue is well conserved among subdomains I and III of eukaryotic Cavs. These findings provide new insight into the Ca2+ selectivity mechanism that is conserved from prokaryotes to eukaryotes. |
| first_indexed | 2024-04-11T09:04:28Z |
| format | Article |
| id | doaj.art-f2aed12e2ac242608410afe16aa57301 |
| institution | Directory Open Access Journal |
| issn | 2050-084X |
| language | English |
| last_indexed | 2024-04-11T09:04:28Z |
| publishDate | 2020-02-01 |
| publisher | eLife Sciences Publications Ltd |
| record_format | Article |
| series | eLife |
| spelling | doaj.art-f2aed12e2ac242608410afe16aa573012022-12-22T04:32:41ZengeLife Sciences Publications LtdeLife2050-084X2020-02-01910.7554/eLife.52828A native prokaryotic voltage-dependent calcium channel with a novel selectivity filter sequenceTakushi Shimomura0https://orcid.org/0000-0002-8109-535XYoshiki Yonekawa1Hitoshi Nagura2Michihiro Tateyama3Yoshinori Fujiyoshi4Katsumasa Irie5https://orcid.org/0000-0002-8178-1552Cellular and Structural Physiology Institute (CeSPI), Nagoya University, Nagoya, Japan; Division of Biophysics and Neurobiology, National Institute for Physiological Sciences, Okazaki, JapanGraduate School of Pharmaceutical Sciences, Nagoya University, Nagoya, JapanCellular and Structural Physiology Institute (CeSPI), Nagoya University, Nagoya, JapanDivision of Biophysics and Neurobiology, National Institute for Physiological Sciences, Okazaki, JapanCellular and Structural Physiology Institute (CeSPI), Nagoya University, Nagoya, Japan; CeSPIA Inc, Tokyo, JapanCellular and Structural Physiology Institute (CeSPI), Nagoya University, Nagoya, Japan; Graduate School of Pharmaceutical Sciences, Nagoya University, Nagoya, JapanVoltage-dependent Ca2+ channels (Cavs) are indispensable for coupling action potentials with Ca2+ signaling in living organisms. The structure of Cavs is similar to that of voltage-dependent Na+ channels (Navs). It is known that prokaryotic Navs can obtain Ca2+ selectivity by negative charge mutations of the selectivity filter, but native prokaryotic Cavs had not yet been identified. We report the first identification of a native prokaryotic Cav, CavMr, whose selectivity filter contains a smaller number of negatively charged residues than that of artificial prokaryotic Cavs. A relative mutant whose selectivity filter was replaced with that of CavMr exhibits high Ca2+ selectivity. Mutational analyses revealed that the glycine residue of the CavMr selectivity filter is a determinant for Ca2+ selectivity. This glycine residue is well conserved among subdomains I and III of eukaryotic Cavs. These findings provide new insight into the Ca2+ selectivity mechanism that is conserved from prokaryotes to eukaryotes.https://elifesciences.org/articles/52828ion selectivityion channelselectrophysiologycalcium channel |
| spellingShingle | Takushi Shimomura Yoshiki Yonekawa Hitoshi Nagura Michihiro Tateyama Yoshinori Fujiyoshi Katsumasa Irie A native prokaryotic voltage-dependent calcium channel with a novel selectivity filter sequence eLife ion selectivity ion channels electrophysiology calcium channel |
| title | A native prokaryotic voltage-dependent calcium channel with a novel selectivity filter sequence |
| title_full | A native prokaryotic voltage-dependent calcium channel with a novel selectivity filter sequence |
| title_fullStr | A native prokaryotic voltage-dependent calcium channel with a novel selectivity filter sequence |
| title_full_unstemmed | A native prokaryotic voltage-dependent calcium channel with a novel selectivity filter sequence |
| title_short | A native prokaryotic voltage-dependent calcium channel with a novel selectivity filter sequence |
| title_sort | native prokaryotic voltage dependent calcium channel with a novel selectivity filter sequence |
| topic | ion selectivity ion channels electrophysiology calcium channel |
| url | https://elifesciences.org/articles/52828 |
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