Two distinct forms of the peridinin-chlorophyll a-protein from Amphidinium carterae.
Peridinin-chlorophyll a-proteins (PCPs) have been purified by combination of ammonium sulphate precipitation and cation exchange chromatography. The amino acid sequences of several of the most abundant forms have been deduced by direct protein sequencing and from DNA and indicate a highly conserved multi-gene family. At least two of the PCP genes are tandemly arranged. A novel form of the protein was also obtained in low yield with fewer peridinins (six vs eight) per chlorophyll a and with a different molecular mass (34 kDa vs 32 kDa) of its apoprotein. It had only 31% sequence identity with any of the more abundant PCP forms but retained a two-domain structure.
Sharples
F P
FP
School of Biological Sciences, Macquarie University, NSW, Australia.
Wrench
P M
PM
Ou
K
K
Hiller
R G
RG
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D002338:Carotenoids / Q000737:chemistry* / Q000235:genetics; D002734:Chlorophyll / Q000737:chemistry* / Q000235:genetics; D000077194:Chlorophyll A; D004141:Dinoflagellida / Q000737:chemistry* / Q000235:genetics; D045342:Light-Harvesting Protein Complexes; D008969:Molecular Sequence Data; D008970:Molecular Weight; D045322:Photosynthetic Reaction Center Complex Proteins / Q000737:chemistry* / Q000235:genetics; D015800:Protozoan Proteins / Q000737:chemistry* / Q000235:genetics; D017421:Sequence Analysis; D017386:Sequence Homology, Amino Acid
D045342:Light-Harvesting Protein Complexes; D045322:Photosynthetic Reaction Center Complex Proteins; D015800:Protozoan Proteins; C073227:peridinin chlorophyll-a protein, Dinophyceae; D002734:Chlorophyll; D002338:Carotenoids; D000077194:Chlorophyll A