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Amino acid sequences of α‐allophycocyanin B from Synechococcus 6301 and Mastigocladus laminosus
Author(s) -
Suter Franz,
Füglistaller Paul,
Lundell Daniel J.,
Glazer Alexander N.,
Zuber Herbert
Publication year - 1987
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(87)80678-6
Subject(s) - allophycocyanin , phycobiliprotein , synechococcus , dodecameric protein , amino acid , biochemistry , peptide sequence , stereochemistry , chemistry , n terminus , biology , cyanobacteria , phycocyanin , bacteria , genetics , dna , gene
The primary structure of α‐allophycocyanin B (α APB ) of Synechococcus 6301 was elucidated. Of the 162 amino acid residues in this polypeptide, 153 were placed by direct sequence determination and the nature of the remaining 9 residues deduced from the amino acid analysis of a peptide generated by the cleavage of α APB with BNPS‐skatole. The probable positions of these 9 residues were assigned by homology to other phycobiliproteins. α APB showed the highest homology, 51%, to α AP . Sequence comparisons suggest that tryptophan residues at positions 60 and 90 in α APB might contribute to the red‐shifted absorption and fluorescence emission maxima of α APB relative to those of α AP . N‐terminal sequences of Mastigocladus laminosus α APB , and Synechococcus 6301 α AP and β AP were also determined. The N‐terminal 55 residues of Synechococcus 6301 β AP isolated from the two complexes (α APB β AP ) 3 and (α AP β AP ) 3 , respectively, were found to be identical.