Evolution of light-harvesting complex proteins from Chl c-containing algae

dc.contributor.authorHoffman, Gabriel E
dc.contributor.authorSanchez-Puerta, M Virginia
dc.contributor.authorDelwiche, Charles F
dc.date.accessioned2021-11-09T14:58:17Z
dc.date.available2021-11-09T14:58:17Z
dc.date.issued2011-04-15
dc.description.abstractLight harvesting complex (LHC) proteins function in photosynthesis by binding chlorophyll (Chl) and carotenoid molecules that absorb light and transfer the energy to the reaction center Chl of the photosystem. Most research has focused on LHCs of plants and chlorophytes that bind Chl a and b and extensive work on these proteins has uncovered a diversity of biochemical functions, expression patterns and amino acid sequences. We focus here on a less-studied family of LHCs that typically bind Chl a and c, and that are widely distributed in Chl c-containing and other algae. Previous phylogenetic analyses of these proteins suggested that individual algal lineages possess proteins from one or two subfamilies, and that most subfamilies are characteristic of a particular algal lineage, but genome-scale datasets had revealed that some species have multiple different forms of the gene. Such observations also suggested that there might have been an important influence of endosymbiosis in the evolution of LHCs. We reconstruct a phylogeny of LHCs from Chl c-containing algae and related lineages using data from recent sequencing projects to give ~10-fold larger taxon sampling than previous studies. The phylogeny indicates that individual taxa possess proteins from multiple LHC subfamilies and that several LHC subfamilies are found in distantly related algal lineages. This phylogenetic pattern implies functional differentiation of the gene families, a hypothesis that is consistent with data on gene expression, carotenoid binding and physical associations with other LHCs. In all probability LHCs have undergone a complex history of evolution of function, gene transfer, and lineage-specific diversification. The analysis provides a strikingly different picture of LHC diversity than previous analyses of LHC evolution. Individual algal lineages possess proteins from multiple LHC subfamilies. Evolutionary relationships showed support for the hypothesized origin of Chl c plastids. This work also allows recent experimental findings about molecular function to be understood in a broader phylogenetic context.en_US
dc.description.urihttps://doi.org/10.1186/1471-2148-11-101
dc.identifierhttps://doi.org/10.13016/nua2-viae
dc.identifier.citationHoffman, G.E., Sanchez-Puerta, M.V. & Delwiche, C.F. Evolution of light-harvesting complex proteins from Chl c-containing algae. BMC Evol Biol 11, 101 (2011).en_US
dc.identifier.urihttp://hdl.handle.net/1903/28097
dc.language.isoen_USen_US
dc.publisherSpringer Natureen_US
dc.relation.isAvailableAtCell Biology & Molecular Geneticsen_us
dc.relation.isAvailableAtDigital Repository at the University of Marylanden_us
dc.relation.isAvailableAtCollege of Computer, Mathematical & Natural Sciencesen_us
dc.relation.isAvailableAtUniversity of Maryland (College Park, MD)en_us
dc.subjectCarotenoiden_US
dc.subjectXanthophyll Cycleen_US
dc.subjectLight Harvesting Complexen_US
dc.subjectFucoxanthinen_US
dc.subjectClade Versusen_US
dc.titleEvolution of light-harvesting complex proteins from Chl c-containing algaeen_US
dc.typeArticleen_US

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