Characterization of a Phycoerythrin without α-Subunits from a Unicellular Red Alga
| Autor: | Jean-Claude Thomas, Chantal Passaquet |
|---|---|
| Rok vydání: | 1999 |
| Předmět: |
Chloroplasts
DNA Complementary Nuclear gene Protein subunit Molecular Sequence Data Restriction Mapping macromolecular substances Biochemistry Chromatography DEAE-Cellulose chemistry.chemical_compound Phycocyanobilin Phycobilisomes Amino Acid Sequence Cloning Molecular Molecular Biology Gene Peptide sequence Base Sequence Sequence Homology Amino Acid biology Phycoerythrin Exons Cell Biology Introns Chloroplast Spectrometry Fluorescence chemistry Rhodophyta biology.protein Phycobilisome |
| Zdroj: | Journal of Biological Chemistry. 274:2472-2482 |
| ISSN: | 0021-9258 |
| DOI: | 10.1074/jbc.274.4.2472 |
| Popis: | We describe here the spectral and biochemical properties of a novel biliprotein belonging to the phycoerythrin family, purified from the phycobilisome of a unicellular red alga, Rhodella reticulata strain R6. This biliprotein is assembled from a unique beta-type subunit, chloroplast-encoded, whose hexameric or dodecameric aggregates are stabilized by unusually large linkers (87 and 60 kDa) encoded by the nuclear genome. Although each beta-type subunit bears two phycoerythrobilins and one phycocyanobilin per chain, the linker polypeptides are non-chromophorylated. The apoprotein of the beta-subunit of the R. reticulata R6 phycoerythrin is specified by a monocistronic rpeB chloroplast gene that is split into three exons. We discuss the relationships between R6 beta-phycoerythrin and the previously published polypeptide sequences, the structural consequences due to the absence of an alpha-subunit, and its evolutionary implications. |
| Databáze: | OpenAIRE |
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