Abstract
The principle light-harvesting chlorophyll a-c-binding protein of Amphidinium carterae of 19 kDa is encoded as a polyprotein translated from a 6.1 kb mRNA. The cDNA sequences indicate that each derived polypeptide is contiguous with the next and that the mature peptides are formed by cleavage at a C-terminal arginine residue. Comparison of the amino-acid sequences shows the Amphidinium protein to be most closely related to the fucoxanthin-chlorophyll-protein (Fcp) of Phaeodactylumand less related to the chlorophyll a-b-binding (Cab) proteins including those from Euglena.
| Original language | English |
|---|---|
| Pages (from-to) | 175-178 |
| Number of pages | 4 |
| Journal | FEBS Letters |
| Volume | 363 |
| Issue number | 1-2 |
| DOIs | |
| Publication status | Published - 17 Apr 1995 |
Keywords
- amino acid sequence
- amphidinium carterae
- chlorophyll c
- dinophyceae
- light-harvesting complex
- polyprotein
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