Color-tuning of natural variants of heliorhodopsin
Microbial rhodopsins are distributed through many microorganisms. Heliorhodopsins are newly discovered but have an unclear function. They have seven transmembrane helices similar to type-I and type-II rhodopsins, but they are different in that the N-terminal region of heliorhodopsin is cytoplasmic....
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| Published in: | Scientific reports Vol. 11; no. 1; pp. 854 - 9 |
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| Main Authors: | , , , , , , |
| Format: | Journal Article |
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| Abstract | Microbial rhodopsins are distributed through many microorganisms. Heliorhodopsins are newly discovered but have an unclear function. They have seven transmembrane helices similar to type-I and type-II rhodopsins, but they are different in that the N-terminal region of heliorhodopsin is cytoplasmic. We chose 13 representative heliorhodopsins from various microorganisms, expressed and purified with an N-terminal His tag, and measured the absorption spectra. The 13 natural variants had an absorption maximum (λmax) in the range 530–556 nm similar to proteorhodopsin (λmax = 490–525 nm). We selected several candidate residues that influence rhodopsin color-tuning based on sequence alignment and constructed mutants via site-directed mutagenesis to confirm the spectral changes. We found two important residues located near retinal chromophore that influence λmax. We also predict the 3D structure via homology-modeling of
Thermoplasmatales
heliorhodopsin. The results indicate that the color-tuning mechanism of type-I rhodopsin can be applied to understand the color-tuning of heliorhodopsin. |
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| AbstractList | Abstract Microbial rhodopsins are distributed through many microorganisms. Heliorhodopsins are newly discovered but have an unclear function. They have seven transmembrane helices similar to type-I and type-II rhodopsins, but they are different in that the N-terminal region of heliorhodopsin is cytoplasmic. We chose 13 representative heliorhodopsins from various microorganisms, expressed and purified with an N-terminal His tag, and measured the absorption spectra. The 13 natural variants had an absorption maximum (λmax) in the range 530–556 nm similar to proteorhodopsin (λmax = 490–525 nm). We selected several candidate residues that influence rhodopsin color-tuning based on sequence alignment and constructed mutants via site-directed mutagenesis to confirm the spectral changes. We found two important residues located near retinal chromophore that influence λmax. We also predict the 3D structure via homology-modeling of Thermoplasmatales heliorhodopsin. The results indicate that the color-tuning mechanism of type-I rhodopsin can be applied to understand the color-tuning of heliorhodopsin. Microbial rhodopsins are distributed through many microorganisms. Heliorhodopsins are newly discovered but have an unclear function. They have seven transmembrane helices similar to type-I and type-II rhodopsins, but they are different in that the N-terminal region of heliorhodopsin is cytoplasmic. We chose 13 representative heliorhodopsins from various microorganisms, expressed and purified with an N-terminal His tag, and measured the absorption spectra. The 13 natural variants had an absorption maximum (λmax) in the range 530–556 nm similar to proteorhodopsin (λmax = 490–525 nm). We selected several candidate residues that influence rhodopsin color-tuning based on sequence alignment and constructed mutants via site-directed mutagenesis to confirm the spectral changes. We found two important residues located near retinal chromophore that influence λmax. We also predict the 3D structure via homology-modeling of Thermoplasmatales heliorhodopsin. The results indicate that the color-tuning mechanism of type-I rhodopsin can be applied to understand the color-tuning of heliorhodopsin. Microbial rhodopsins are distributed through many microorganisms. Heliorhodopsins are newly discovered but have an unclear function. They have seven transmembrane helices similar to type-I and type-II rhodopsins, but they are different in that the N-terminal region of heliorhodopsin is cytoplasmic. We chose 13 representative heliorhodopsins from various microorganisms, expressed and purified with an N-terminal His tag, and measured the absorption spectra. The 13 natural variants had an absorption maximum (λmax) in the range 530-556 nm similar to proteorhodopsin (λmax = 490-525 nm). We selected several candidate residues that influence rhodopsin color-tuning based on sequence alignment and constructed mutants via site-directed mutagenesis to confirm the spectral changes. We found two important residues located near retinal chromophore that influence λmax. We also predict the 3D structure via homology-modeling of Thermoplasmatales heliorhodopsin. The results indicate that the color-tuning mechanism of type-I rhodopsin can be applied to understand the color-tuning of heliorhodopsin. Microbial rhodopsins are distributed through many microorganisms. Heliorhodopsins are newly discovered but have an unclear function. They have seven transmembrane helices similar to type-I and type-II rhodopsins, but they are different in that the N-terminal region of heliorhodopsin is cytoplasmic. We chose 13 representative heliorhodopsins from various microorganisms, expressed and purified with an N-terminal His tag, and measured the absorption spectra. The 13 natural variants had an absorption maximum (λmax) in the range 530–556 nm similar to proteorhodopsin (λmax = 490–525 nm). We selected several candidate residues that influence rhodopsin color-tuning based on sequence alignment and constructed mutants via site-directed mutagenesis to confirm the spectral changes. We found two important residues located near retinal chromophore that influence λmax. We also predict the 3D structure via homology-modeling of Thermoplasmatales heliorhodopsin. The results indicate that the color-tuning mechanism of type-I rhodopsin can be applied to understand the color-tuning of heliorhodopsin. |
| ArticleNumber | 854 |
| Author | Choi, Ahreum Chuon, Kimleng Jung, Kwang-Hwan Kim, Se-Hwan Cho, Shin-Gyu Cho, Hyun-Suk Meas, Seanghun |
| Author_xml | – sequence: 1 givenname: Se-Hwan surname: Kim fullname: Kim, Se-Hwan organization: Department of Life Science and Institute of Biological Interfaces, Sogang University – sequence: 2 givenname: Kimleng surname: Chuon fullname: Chuon, Kimleng organization: Department of Life Science and Institute of Biological Interfaces, Sogang University – sequence: 3 givenname: Shin-Gyu surname: Cho fullname: Cho, Shin-Gyu organization: Department of Life Science and Institute of Biological Interfaces, Sogang University – sequence: 4 givenname: Ahreum surname: Choi fullname: Choi, Ahreum organization: Research Center for Endangered Species, National Institute of Ecology – sequence: 5 givenname: Seanghun surname: Meas fullname: Meas, Seanghun organization: Department of Life Science and Institute of Biological Interfaces, Sogang University – sequence: 6 givenname: Hyun-Suk surname: Cho fullname: Cho, Hyun-Suk organization: Department of Life Science and Institute of Biological Interfaces, Sogang University – sequence: 7 givenname: Kwang-Hwan surname: Jung fullname: Jung, Kwang-Hwan email: kjung@sogang.ac.kr organization: Department of Life Science and Institute of Biological Interfaces, Sogang University |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/33441566$$D View this record in MEDLINE/PubMed |
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| CitedBy_id | crossref_primary_10_1021_acs_jpcb_4c00804 crossref_primary_10_1021_acs_jpclett_4c00879 crossref_primary_10_1016_j_mrl_2024_200132 crossref_primary_10_1111_1462_2920_15890 crossref_primary_10_1038_s41598_022_17716_9 crossref_primary_10_3390_ijms242417269 |
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| SubjectTerms | 631/326 631/45 631/57 Absorption Chromophores Color vision Homology Humanities and Social Sciences Microorganisms multidisciplinary Nucleotide sequence Rhodopsin Science Science (multidisciplinary) Site-directed mutagenesis |
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| Title | Color-tuning of natural variants of heliorhodopsin |
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