Amino acid sequences of α‐allophycocyanin B from Synechococcus 6301 and Mastigocladus laminosus

FEBS Letters

Zuber, Herbert¹  Glazer, Alexander N.²  Füglistaller, Paul¹  Suter, Franz¹  Lundell, Daniel J.² 

[1] >Institut für Molekularbiologie und Biophysik, Eidgenössische Technische Hochschule, CH-8093 Zürich, Switzerland;Department of Microbiology and Immunology, University of California, Berkeley, CA 94720, USA

关键词: α-Allophycocyanin B;    Phycobiliprotein;    Amino acid sequence;    (Synechococcus 6301;    Mastigocladus laminosus);    BNPS-skatole;    2-(2-nitrophenylsulfenyl)-3-methylbromoindolenine;    phycobiliprotein subunits and linker polypeptides of phycobilisomes are abbreviated as described by Glazer [(1985) Annu. Rev. Biophys. Biophys. Chem. 14;    47-77];    AP;    allophycocyanin;   

DOI  :  10.1016/0014-5793(87)80678-6

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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^APBβ^AP)₃ and (α^APβ^AP)₃, respectively, were found to be identical.

【 授权许可】

Unknown