Molecular and General Genetics MGG

, Volume 253, Issue 3, pp 377–386

The fucoxanthin-chlorophyll proteins from a chromophyte alga are part of a large multigene family: structural and evolutionary relationships to other light harvesting antennae


  • D. G. Durnford
    • Botany Dept., University of British Columbia, Vancouver, British Columbia, Canada, V6T 1Z4.
  • R. Aebersold
    • Department of Molecular Biotechnology, University of Washington, Seattle, WA 98104, USA
  • B. R. Green
    • Botany Dept., University of British Columbia, Vancouver, British Columbia, Canada, V6T 1Z4.

DOI: 10.1007/s004380050334

Cite this article as:
Durnford, D., Aebersold, R. & Green, B. Mol Gen Genet (1996) 253: 377. doi:10.1007/s004380050334


 A fucoxanthin-chlorophyll protein (FCP) cDNA from the raphidophyte Heterosigma carterae encodes a 210-amino acid polypeptide that has similarity to other FCPs and to the chlorophyll a/b-binding proteins (CABs) of terrestrial plants and green algae. The putative transit sequence has characteristics that resemble a signal sequence. The Heterosigma fcp genes are part of a large multigene family which includes members encoding at least two significantly different polypeptides (Fcp1, Fcp2). Comparison of the FCP sequences to the recently determined three-dimensional structure of the pea LHC II complex indicates that many of the key amino acids thought to participate in the binding of chlorophyll and the formation of complex-stabilizing ionic interactions are well conserved. Phylogenetic analyses of sequences of light-harvesting proteins shows that the FCPs of several chromophyte phyla form a natural group separate from the intrinisic peridinin-chlorophyll proteins (iPCPs) of the dinoflagellates. Although the FCP and CAB genes shared a common ancestor, these lineages diverged from each other prior to the separation of the CAB LHC I and LHC II sequences in the green algae and terrestrial plants.

Key words Light-harvesting antennaeMolecular evolutionHeterosigma carteraeFucoxanthinGene family

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© Springer-Verlag Berlin Heidelberg 1996