A minimal phycobilisome: fusion and chromophorylation of the truncated core-membrane linker and phycocyanin.

Kun Tang, Xiao-Li Zeng, Yi Yang, Zhi-Bin Wang, Xian-Jun Wu, Ming Zhou, Dror Noy, Hugo Scheer, Kai-Hong Zhao, Kun Tang, Xiao-Li Zeng, Yi Yang, Zhi-Bin Wang, Xian-Jun Wu, Ming Zhou, Dror Noy, Hugo Scheer, Kai-Hong Zhao

Index: Biochim. Biophys. Acta 1817(7) , 1030-6, (2012)

Full Text: HTML

Abstract

Phycobilisomes, the light-harvesting antennas in cyanobacteria and red algae, consist of an allophycocyanin core that is attached to the membrane via a core-membrane linker, and rods comprised of phycocyanin and often also phycoerythrin or phycoerythrocyanin. Phycobiliproteins show excellent energy transfer among the chromophores that renders them biomarkers with large Stokes-shifts absorbing over most of the visible spectrum and into the near infrared. Their application is limited, however, due to covalent binding of the chromophores and by solubility problems. We report construction of a water-soluble minimal chromophore-binding unit of the red-absorbing and fluorescing core-membrane linker. This was fused to minimal chromophore-binding units of phycocyanin. After double chromophorylation with phycocyanobilin, in E. coli, the fused phycobiliproteins absorbed light in the range of 610-660nm, and fluoresced at ~670nm, similar to phycobilisomes devoid of phycoerythr(ocyan)in. The fused phycobiliprotein could also be doubly chromophorylated with phycoerythrobilin, resulting in a chromoprotein absorbing around 540-575nm, and fluorescing at ~585nm. The broad absorptions and the large Stokes shifts render these chromoproteins candidates for imaging; they may also be helpful in studying phycobilisome assembly.Copyright © 2012 Elsevier B.V. All rights reserved.