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Structure, Diversity, and Evolution of a New Family of Soluble Carotenoid-Binding Proteins in Cyanobacteria

Molecular Plant 2016年第10期9卷 1379-1394页

作者： Matthew R. Melnicki Ryan L. Leverenz Markus Sutter Rocio Lopez-lgual Adjele Wilson Emily G. Pawlowski Francois Perreau diana kirilovsky Cheryl A. Kerfeld Department of Plant and Microbial Biology University of California Berkeley CA 94720 USA Physical Biosciences Division Lawrence Berkeley National Laboratory Berkeley CA 94720 USA MSU-DOE Plant Research Laboratory Department of Biochemistry and Molecular Biology Michigan State University East Lansing MI 48824 USA Institute for Integrative Biology of the Cell (I2BC) CEA CNRS Universite Paris-Sud Universite Paris-Saclay 91198 Gif-sur-Yvette France Commissariat & I'Energie Atomique (CEA) Institut de Biologie et Technologies de Saclay (iBiTec-S) 91191 Gif-sur-Yvette France INRA Institut Jean-Pierre Bourgin UMR 1318 ERL CNRS 3559 Saclay Plant Sciences RD10 78026 Versailles France Unite Plasticite du Genome Bacterien Departement Genomes et Genetique Institut Pasteur CNRS Unite Mixte de Recherche 3525 75015 Paris France

Using a phylogenomic approach, we have identified and subciassified a new family of carotenoid-binding proteins. These proteins have sequence homology to the N-terminal domain （NTD） of the Orange Carotenoid Protein （OCP）, and are referred to as Helical Carotenoid Proteins （HCPs）. These proteins comprise at least nine distinct ciades and are found in diverse organisms, frequently as multiple paralogs representing the distinct ciades. These seem to be out-paralogs maintained from ancient duplications associated with subfunctionalization. All of the HCPs share conservation of the residues for carotenoid binding, and we confirm that carotenoid binding is a fundamental property of HCPso We solved two crystal structures of the Nostoc sp. PCC 7120 HCP1 protein, each binding a different carotenoid, suggesting that the proteins flexibly bind a range of carotenoids. Based on a comprehensive phylogenetic analysis, we propose that one of the HCP subtypes is likely the evolutionary ancestor of the NTD of the OCP, which arose following a domain fusion evenS. However, we predict that the majority of HCPs have functions distinct from the NTD of the OCP. Our results demonstrate that the HCPs are a new family of functionally diverse carotenoid-binding proteins found among ecophysiologically diverse cyanobacteria.

关键词： carotenoids cyanobacteria phylogenomics protein structure photoprotection molecular evolution

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