The Complete Amino-Acid Sequence of the α and β Subunits of B-Phycoerythrin from the Rhodophytan AlgaPorphyridium Cruentum
- 1 January 1989
- journal article
- research article
- Published by Walter de Gruyter GmbH in Biological Chemistry Hoppe-Seyler
- Vol. 370 (1) , 115-124
- https://doi.org/10.1515/bchm3.1989.370.1.115
Abstract
Determination of the complete amino-acid sequence of the subunits of B-phycoerythrin from Porphyridium cruentum has shown that the .alpha. subunit contains 164 amino-acid residues and the .beta. subunit contains 177 residues. When the sequences of B- and C-phycoerythrins are aligned with those of other phycobiliproteins, it is obvious that B-phycoerythrin lacks a deletion at .beta.-21-22 present in C-phycoerythrin. However, relative to C-phycoerythrin from Fremyella diplosiphon (Calothrix) (Sidler, W., Kumpf, B., Rudiger, W. and Zuber, H. (1986) Biol. Chem. Hoppe-Syeler 367, 627-642), B-phycoerythrin has deletions at .beta.-141k-o, .beta.-142, .beta.-143, .beta.-147, .beta.-148. The four singly-linked phycoerythrobilins at positions .alpha.-84, .alpha.-143a, .beta.-84 and .beta.-155, and the doubly-linked phycoerythrobilin at position .beta.-50/61 are at sites homologous to the attachment sites in C-phycoerythrin. The aspartyl residues (.alpha.-87, .beta.-87, and .beta.-39), that interact with the bilins at .alpha.-84, .beta.-84, and .beta.-155 in C-phycocyanin, are found in the homologous positions in B-phycoerythrin. B-Phycoerythrin, in common with other phycobiliproteins, contains a N.gamma.-methylasparagine residue at position .beta.-72.This publication has 34 references indexed in Scilit:
- Refined three-dimensional structures of two cyanobacterial C-phycocyanins at 2.1 and 2.5 Å resolutionJournal of Molecular Biology, 1987
- Isolation and Localization ofN-Methylasparagine in Phycobiliproteins from the CyanobacteriumMastigocladus laminosusBiological Chemistry Hoppe-Seyler, 1987
- The Complete Amino-Acid Sequence of C-Phycoerythrin from the CyanobacteriumFremyella diplosiphonBiological Chemistry Hoppe-Seyler, 1986
- The Primary Structure ofBacillus cereusNeutral Proteinase and Comparison with Thermolysin andBacillus subtilisNeutral ProteinaseBiological Chemistry Hoppe-Seyler, 1986
- X-ray crystallographic structure of the light-harvesting biliprotein C-phycocyanin from the thermophilic cyanobacterium Mastigocladus laminosus and its resemblance to globin structuresJournal of Molecular Biology, 1985
- Minor Polypeptides from the Phycobilisome of the CyanobacteriumMastigocladus laminosus.Isolation, Characterization and Amino-Acid Sequences of a Colourless 8.9-kDa Polypeptide and of a 16.2-kDa PhycobiliproteinHoppe-Seyler´s Zeitschrift Für Physiologische Chemie, 1984
- Chromopeptides from phycoerythrins. Structure and linkage of a phycoerythrobilin tryptic tripeptide derived from a B-phycoerythrinJournal of the American Chemical Society, 1983
- The Complete Amino Acid Sequence of Both Subunits of C-Phycocyanin from the CyanobacteriumMastigocladus laminosusHoppe-Seyler´s Zeitschrift Für Physiologische Chemie, 1978
- The quaternary structure of a unique phycobiliprotein: B-phycoerythrin from Porphyridium cruentumBiochemical and Biophysical Research Communications, 1977
- The Complete Amino Acid Sequences of Both Subunits of the Sweet Protein MonellinHoppe-Seyler´s Zeitschrift Für Physiologische Chemie, 1976