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Autori principali: Hasegawa-Takano, Masumi, Hosaka, Toshiaki, Kojima, Keiichi, Nishimura, Yosuke, Kurihara, Marie, Nakajima, Yu, Ishizuka-Katsura, Yoshiko, Kimura-Someya, Tomomi, Shirouzu, Mikako, Sudo, Yuki, Yoshizawa, Susumu
Natura: Artículo científico
Lingua:en
Pubblicazione: The ISME journal 2024
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Accesso online:https://pubmed.ncbi.nlm.nih.gov/39485071/
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author Hasegawa-Takano, Masumi
Hosaka, Toshiaki
Kojima, Keiichi
Nishimura, Yosuke
Kurihara, Marie
Nakajima, Yu
Ishizuka-Katsura, Yoshiko
Kimura-Someya, Tomomi
Shirouzu, Mikako
Sudo, Yuki
Yoshizawa, Susumu
author_facet Hasegawa-Takano, Masumi
Hosaka, Toshiaki
Kojima, Keiichi
Nishimura, Yosuke
Kurihara, Marie
Nakajima, Yu
Ishizuka-Katsura, Yoshiko
Kimura-Someya, Tomomi
Shirouzu, Mikako
Sudo, Yuki
Yoshizawa, Susumu
Hasegawa-Takano, Masumi
Hosaka, Toshiaki
Kojima, Keiichi
Nishimura, Yosuke
Kurihara, Marie
Nakajima, Yu
Ishizuka-Katsura, Yoshiko
Kimura-Someya, Tomomi
Shirouzu, Mikako
Sudo, Yuki
Yoshizawa, Susumu
collection PubMed - marine biology
contents Cyanorhodopsin-II represents a yellow-absorbing proton-pumping rhodopsin clade within cyanobacteria. Hasegawa-Takano, Masumi Hosaka, Toshiaki Kojima, Keiichi Nishimura, Yosuke Kurihara, Marie Nakajima, Yu Ishizuka-Katsura, Yoshiko Kimura-Someya, Tomomi Shirouzu, Mikako Sudo, Yuki Yoshizawa, Susumu Cyanobacteria Phylogeny Rhodopsins, Microbial Proton Pumps Bacterial Proteins Light Metagenomics Microbial rhodopsins are prevalent in many cyanobacterial groups as a light-energy-harvesting system in addition to the photosynthetic system. It has been suggested that this dual system allows efficient capture of sunlight energy using complementary ranges of absorption wavelengths. However, the diversity of cyanobacterial rhodopsins, particularly in accumulated metagenomic data, remains underexplored. Here, we used a metagenomic mining approach, which led to the identification of a novel rhodopsin clade unique to cyanobacteria, cyanorhodopsin-II (CyR-II). CyR-IIs function as light-driven outward H+ pumps. CyR-IIs, together with previously identified cyanorhodopsins (CyRs) and cyanobacterial halorhodopsins (CyHRs), constitute cyanobacterial ion-pumping rhodopsins (CyipRs), a phylogenetically distinct family of rhodopsins. The CyR-II clade is further divided into two subclades, YCyR-II and GCyR-II, based on their specific absorption wavelength. YCyR-II absorbed yellow light (λmax = 570 nm), whereas GCyR-II absorbed green light (λmax = 550 nm). X-ray crystallography and mutational analysis revealed that the difference in absorption wavelengths is attributable to slight changes in the side chain structure near the retinal chromophore. The evolutionary trajectory of cyanobacterial rhodopsins suggests that the function and light-absorbing range of these rhodopsins have been adapted to a wide range of habitats with variable light and environmental conditions. Collectively, these findings shed light on the importance of rhodopsins in the evolution and environmental adaptation of cyanobacteria.
format Artículo científico
id pubmed_39485071
institution PubMed
language en
publishDate 2024
publisher The ISME journal
record_format pubmed
spellingShingle Cyanorhodopsin-II represents a yellow-absorbing proton-pumping rhodopsin clade within cyanobacteria.
Hasegawa-Takano, Masumi
Hosaka, Toshiaki
Kojima, Keiichi
Nishimura, Yosuke
Kurihara, Marie
Nakajima, Yu
Ishizuka-Katsura, Yoshiko
Kimura-Someya, Tomomi
Shirouzu, Mikako
Sudo, Yuki
Yoshizawa, Susumu
Cyanobacteria
Phylogeny
Rhodopsins, Microbial
Proton Pumps
Bacterial Proteins
Light
Metagenomics
Cyanorhodopsin-II represents a yellow-absorbing proton-pumping rhodopsin clade within cyanobacteria. Hasegawa-Takano, Masumi Hosaka, Toshiaki Kojima, Keiichi Nishimura, Yosuke Kurihara, Marie Nakajima, Yu Ishizuka-Katsura, Yoshiko Kimura-Someya, Tomomi Shirouzu, Mikako Sudo, Yuki Yoshizawa, Susumu Cyanobacteria Phylogeny Rhodopsins, Microbial Proton Pumps Bacterial Proteins Light Metagenomics Microbial rhodopsins are prevalent in many cyanobacterial groups as a light-energy-harvesting system in addition to the photosynthetic system. It has been suggested that this dual system allows efficient capture of sunlight energy using complementary ranges of absorption wavelengths. However, the diversity of cyanobacterial rhodopsins, particularly in accumulated metagenomic data, remains underexplored. Here, we used a metagenomic mining approach, which led to the identification of a novel rhodopsin clade unique to cyanobacteria, cyanorhodopsin-II (CyR-II). CyR-IIs function as light-driven outward H+ pumps. CyR-IIs, together with previously identified cyanorhodopsins (CyRs) and cyanobacterial halorhodopsins (CyHRs), constitute cyanobacterial ion-pumping rhodopsins (CyipRs), a phylogenetically distinct family of rhodopsins. The CyR-II clade is further divided into two subclades, YCyR-II and GCyR-II, based on their specific absorption wavelength. YCyR-II absorbed yellow light (λmax = 570 nm), whereas GCyR-II absorbed green light (λmax = 550 nm). X-ray crystallography and mutational analysis revealed that the difference in absorption wavelengths is attributable to slight changes in the side chain structure near the retinal chromophore. The evolutionary trajectory of cyanobacterial rhodopsins suggests that the function and light-absorbing range of these rhodopsins have been adapted to a wide range of habitats with variable light and environmental conditions. Collectively, these findings shed light on the importance of rhodopsins in the evolution and environmental adaptation of cyanobacteria.
title Cyanorhodopsin-II represents a yellow-absorbing proton-pumping rhodopsin clade within cyanobacteria.
topic Cyanobacteria
Phylogeny
Rhodopsins, Microbial
Proton Pumps
Bacterial Proteins
Light
Metagenomics
url https://pubmed.ncbi.nlm.nih.gov/39485071/