The accessory light-harvesting polypeptides associated with photosystem I (LHCI) in Porphyridium cruentum bind chlorophyll a, zeaxanthin and β-carotene. A cDNA library of P. cruentum was screened with an antiserum specific to the LHCI polypeptides, and an 0.9 kb fragment was identified as coding for an LHCI polypeptide. This cDNA, which we named LhcaR1, has an open reading frame encoding 222 amino acid residues including a putative transit peptide of 28 amino acids. Hydropathy analysis suggests that there are three transmembrane helices in the mature polypeptide. Each of the amino acid residues that bind chlorophyll (six residues) and serve in stabilizing the helices in higher-plant LHCs are conserved in helices 1 and 3 of P. cruentum LhcaR1. The N-terminal flanking regions of these two helices also show high sequence conservation with other LHCs. Helix 2 contains a seventh putative chlorophyll-binding site, but resembles helix 2 of higher-plant LHCs to a lesser degree. A sequence motif of 11 residues found near the N-terminus and in each of the three helices suggests the possibility that the red algal LhcaR1 derives from a gene duplication. Polypeptides of the expected molecular weight in six other red algae (Achrochaetium, Bangia, Callithamnion, Cyanidium, Polysiphonia, Spermothamnion) were recognized by the antiserum to P. cruentum LHCI, indicating a wide distribution of LHCI in rhodophytes.
Plant Molecular Biology – Springer Journals
Published: Sep 29, 2004
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