The 15-kDa forms of the apo-peridinin-chlorophyll a protein (PCP) in dinoflagellates show high identity with the apo-32 kDa PCP forms, and have similar N-terminal leaders and gene arrangements
| Autor: | Roger G. Hiller, Pamela M. Wrench, N. Santucci, Eckhard Hofmann, L. G. Crossley |
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| Rok vydání: | 2001 |
| Předmět: |
Models
Molecular Signal peptide DNA Complementary Molecular Sequence Data Protozoan Proteins Trimer Protein Sorting Signals Biology chemistry.chemical_compound Gene Order Genetics Animals Protein Isoforms Molecular Biology Gene Peptide sequence Sequence (medicine) Base Sequence Sequence Homology Amino Acid Amphidinium Intron Sequence Analysis DNA General Medicine DNA Protozoan biology.organism_classification Carotenoids Molecular Weight Peridinin Biochemistry chemistry Dinoflagellida Dimerization Sequence Alignment |
| Zdroj: | Molecular Genetics and Genomics. 266:254-259 |
| ISSN: | 1617-4623 1617-4615 |
| DOI: | 10.1007/s004380100551 |
| Popis: | Full-length genomic sequences encoding apo peridinin-chlorophyll a proteins (PCPs) from Heterocapsa pygmaea have been obtained by PCR. Two of the derived mature proteins of 150 residues have molecular masses of 15,795 and 15,780, respectively. Contrary to an earlier report, these show a high degree of identity (approximately 70%) over the whole of both domains to the mature 32-kDa PCP forms. The two genes lack introns, are arranged in tandem and separated by 526 bp. A putative N-terminal extension with three domains characteristic of a signal sequence, a chloroplast-targeting sequence and a thylakoid lumen-directing sequence, is present. Modelling of the Heterocapsa PCP amino acid sequence on to the high-resolution structure available for Amphidinium PCP shows that the main differences between two forms are in trimer contact regions. |
| Databáze: | OpenAIRE |
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