학술논문

Molecular phylogeny of fucoxanthin-chlorophyll a/c proteins from Chaetoceros gracilis and Lhcq/Lhcf diversity.
Document Type
Academic Journal
Author
Kumazawa M; Graduate School of Biostudies, Kyoto University, Kyoto, Japan.; Nishide H; National Institute for Basic Biology, National Institutes of Natural Sciences, Aichi, Japan.; Nagao R; Research Institute for Interdisciplinary Science and Graduate School of Natural Science and Technology, Okayama University, Okayama, Japan.; Inoue-Kashino N; Graduate School of Life Science, University of Hyogo, Hyogo, Japan.; Shen JR; Research Institute for Interdisciplinary Science and Graduate School of Natural Science and Technology, Okayama University, Okayama, Japan.; Nakano T; Graduate School of Biostudies, Kyoto University, Kyoto, Japan.; Uchiyama I; National Institute for Basic Biology, National Institutes of Natural Sciences, Aichi, Japan.; Kashino Y; Graduate School of Life Science, University of Hyogo, Hyogo, Japan.; Ifuku K; Graduate School of Agriculture, Kyoto University, Kyoto, Japan.
Source
Publisher: Scandinavian Society For Plant Physiology Country of Publication: Denmark NLM ID: 1256322 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1399-3054 (Electronic) Linking ISSN: 00319317 NLM ISO Abbreviation: Physiol Plant Subsets: MEDLINE
Subject
Language
English
Abstract
Diatoms adapt to various aquatic light environments and play major roles in the global carbon cycle using their unique light-harvesting system, i.e. fucoxanthin chlorophyll a/c binding proteins (FCPs). Structural analyses of photosystem II (PSII)-FCPII and photosystem I (PSI)-FCPI complexes from the diatom Chaetoceros gracilis have revealed the localization and interactions of many FCPs; however, the entire set of FCPs has not been characterized. Here, we identify 46 FCPs in the newly assembled genome and transcriptome of C. gracilis. Phylogenetic analyses suggest that these FCPs can be classified into five subfamilies: Lhcr, Lhcf, Lhcx, Lhcz, and the novel Lhcq, in addition to a distinct type of Lhcr, CgLhcr9. The FCPs in Lhcr, including CgLhcr9 and some Lhcqs, have orthologous proteins in other diatoms, particularly those found in the PSI-FCPI structure. By contrast, the Lhcf subfamily, some of which were found in the PSII-FCPII complex, seems to be diversified in each diatom species, and the number of Lhcqs differs among species, indicating that their diversification may contribute to species-specific adaptations to light. Further phylogenetic analyses of FCPs/light-harvesting complex (LHC) proteins using genome data and assembled transcriptomes of other diatoms and microalgae in public databases suggest that our proposed classification of FCPs is common among various red-lineage algae derived from secondary endosymbiosis of red algae, including Haptophyta. These results provide insights into the loss and gain of FCP/LHC subfamilies during the evolutionary history of the red algal lineage.
(© 2021 Scandinavian Plant Physiology Society.)