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Plant and Cell Physiology Advance Access published online on February 2, 2005
Plant and Cell Physiology, doi:10.1093/pcp/pci054
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Plant and Cell Physiology 2005 © The Japanese Society of Plant Physiologists (JSPP); all rights reserved.
Received March 23, 2004
Revised December 10, 2004
Accepted January 11, 2005

Regular Paper

Isolation of a Novel Carotenoid-Rich Protein in Cyanophora paradoxa that Is Immunologically Related to the Light-Harvesting Complexes of Photosynthetic Eukaryotes

Heather M. Rissler 1 and Dion G. Durnford 1*

1 Department of Biology, University of New Brunswick, Fredericton, New Brunswick, Canada, E3B 6E1

* To whom correspondence should be addressed.
Dion G. Durnford, E-mail: durnford{at}unb.ca


  Abstract

Novel eukaryotic chlorophyll-carotenoid proteins have evolved at least twice following the origin of the plastid and include the widely distributed integral membrane light harvesting complexes (LHCs) and the dinoflagellate-specific soluble peridinin-chlorophyll proteins. In the glaucophytes, homologues of these proteins are reportedly absent. We have identified a novel carotenoid-rich protein (CRP) in the glaucophyte Cyanophora paradoxa that is 28 kDa and immunologically related to the family of LHCs. CRP is associated with the thylakoid membrane, though it can be removed by stringent washes suggesting that there are likely significant structural differences between CRP and the LHCs. CRP co-localizes with a zeaxanthin-rich thylakoid membrane fraction that also contains {beta}-carotene, chlorophyll and an unidentified carotenoid. Despite this, we found no evidence for carotenoid-chlorophyll energy transfer in the isolated complex, suggesting light-harvesting may not be a primary function. The presence of CRP in C. paradoxa is evidence for the evolution of a novel pigment-binding protein in the glaucophytes.

Keywords: Cyanophora paradoxa; pigment-binding protein; light-harvesting complex; plastid evolution; zeaxanthin.
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