The complete amino acid sequence of R-phycocyanin-I alpha and beta subunits from the red alga Porphyridium cruentum. Structural and phylogenetic relationships of the phycocyanins within the phycobiliprotein families
| Autor: | Walter Sidler, Gerhard Frank, Herbert Zuber, Axel Ducret |
|---|---|
| Rok vydání: | 1994 |
| Předmět: |
Molecular Sequence Data
Light-Harvesting Protein Complexes Phycoerythrobilin macromolecular substances Cyanobacteria Methylation Biochemistry chemistry.chemical_compound Bacterial Proteins Phycocyanobilin Phycocyanin Amino Acid Sequence Peptide sequence Chromatography High Pressure Liquid Phylogeny Plant Proteins Binding Sites Sequence Homology Amino Acid biology Phycobiliprotein Phycoerythrocyanin Pigments Biological biology.organism_classification Spectrometry Fluorescence chemistry Porphyridium cruentum Rhodophyta biology.protein Asparagine Sequence Analysis Phycoerythrin |
| Zdroj: | European Journal of Biochemistry. 221:563-580 |
| ISSN: | 1432-1033 0014-2956 |
| Popis: | We present here the complete primary structure of R-phycocyanin-I alpha and beta subunits from the red alga Porphyridium cruentum. The alpha chain is composed of 162 amino acid residues (18049 Da, calculated from sequence, including chromophore) and carries a phycocyanobilin pigment covalently linked to Cys84. The beta chain contains 172 amino acids (19344Da, calculated from sequence, including chromophores) and carries a phycocyanobilin pigment covalently linked at Cys82 and a phycoerythrobilin pigment at Cys153. A gamma-N-methyl asparagine residue was also characterised at position beta 72 similar to other phycobiliprotein beta subunits. R-phycocyanin-I from Porphyridium cruentum shares high sequence identity with C-phycocyanins (69-83%), R-phycocyanins (66-70%) and in a less extent with phycoerythrocyanins (57-65%) from various sources. The presented phylogenetic trees are based on a comparison of all phycobiliprotein amino acid sequences known so far and confirm the clear affiliation of the R-phycocyanins in the phycocyanin family. In spite of their particular phycobilin pattern, they do not represent intermediate forms between the phycocyanin and the phycoerythrin family. Phycoerythrocyanin, a phycocyanin-related phycobiliprotein adapted to green light harvesting, is also shown to belong to the phycocyanin family. However, the phycoerythrocyanins diverge from phycocyanins in their different function and it is suggested that they should be assigned to a separate group within the phycocyanin family. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|