Skip Navigation


Plant and Cell Physiology Advance Access originally published online on February 2, 2005
Plant and Cell Physiology 2005 46(3):416-424; doi:10.1093/pcp/pci054
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
46/3/416    most recent
pci054v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in ISI Web of Science
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Search for citing articles in:
ISI Web of Science (2)
Right arrowRequest Permissions
Google Scholar
Right arrow Articles by Rissler, H. M.
Right arrow Articles by Durnford, D. G.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Rissler, H. M.
Right arrow Articles by Durnford, D. G.
Agricola
Right arrow Articles by Rissler, H. M.
Right arrow Articles by Durnford, D. G.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

JSPP © 2005

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 and Dion G. Durnford1

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

1 Corresponding author: E-mail, durnford{at}unb.ca; Fax, +1-506-453-3583.

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, homologs 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 probably significant structural differences between CRP and the LHCs. CRP co-localizes with a zeaxanthin-rich thylakoid membrane fraction that also contains ß-carotene, chlorophyll and an unidentified carotenoid. Despite this, we found no evidence for carotenoid–chlorophyll energy transfer in the isolated complex, suggesting that 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.

Received March 23, 2004; Accepted December 10, 2004
Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
 Phil Trans R Soc BHome page
C.J Howe, A.C Barbrook, R.E.R Nisbet, P.J Lockhart, and A.W.D Larkum
The origin of plastids
Phil Trans R Soc B, August 27, 2008; 363(1504): 2675 - 2685.
[Abstract] [Full Text] [PDF]

Home page
 Plant Physiol.Home page
A. G. Koziol, T. Borza, K.-I. Ishida, P. Keeling, R. W. Lee, and D. G. Durnford
Tracing the Evolution of the Light-Harvesting Antennae in Chlorophyll a/b-Containing Organisms
Plant Physiology, April 1, 2007; 143(4): 1802 - 1816.
[Abstract] [Full Text] [PDF]


Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.