RESEARCH ARTICLE The γ33 subunit of R-phycoerythrin from Gracilaria chilensis has a typical double linked phycourobilin similar to γ subunit Aleikar VaÂsquez-SuaÂrez1☯, Francisco Lobos-GonzaÂlez1☯, Andrew Cronshaw2, Jose Sepu lveda-Ugarte1, Maximiliano Figueroa1, Jorge Dagnino-Leone1, Marta Bunster1*, Jose MartõÂnez-Oyanedel1* 1 Laboratorio de BiofõÂsica Molecular, Departamento de BioquõÂmica y BiologõÂa Molecular, Facultad de Ciencias BioloÂgicas Universidad de ConcepcioÂn, ConcepcioÂn, Chile, 2 Michael Swann Building, Kings' a1111111111 Buildings, University of Edinburgh, Edinburgh, Scotland, United Kingdom a1111111111 a1111111111 ☯ These authors contributed equally to this work. a1111111111 *
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[email protected] (JM-O) a1111111111 Abstract Phycobilisomes (PBS) are accessory light harvesting protein complexes formed mainly by OPEN ACCESS phycobiliproteins (PBPs). The PBPs absorb light that is efficiently transferred to Photosys- Citation: VaÂsquez-SuaÂrez A, Lobos-GonzaÂlez F, tems due to chromophores covalently bound to specific cysteine residues. Besides phycobi- Cronshaw A, SepuÂlveda-Ugarte J, Figueroa M, liproteins (PE), the PBS contains linker proteins responsible for assembly and stabilization 33 Dagnino-Leone J, et al. (2018) The γ subunit of of the whole complex and the tuning of energy transfer steps between chromophores. The R-phycoerythrin from Gracilaria chilensis has a 33 typical double linked phycourobilin similar to γ linker (γ ) from Gracilaria chilensis, is a chromophorylated rod linker associated to (αβ)6 subunit. PLoS ONE 13(4): e0195656. https://doi. hexamers of R-phycoerythrin (R-PE). Its role in the energy transfer process is not clear yet. org/10.1371/journal.pone.0195656 Structural studies as well as the composition and location of the chromophores are essential Editor: Peter Butko, Nagoya University, JAPAN to understand their involvement in the energy transfer process in PBS.