Three C‐phycoerythrin‐associated linker polypeptides in the phycobilisome of green‐light‐grown Calothrix sp. PCC 7601 (cyanobacteria)

FEBS Letters

Graham, Karl W.¹  Zuber, Herbert¹  Frank, Gerhard¹  Glauser, Manuel¹  Wehrli, Ernst¹  Sidler, Walter A.¹  Bryant, Donald A.¹ 

[1]Institut für Molekularbiologie und Biophysik, Eidgenössische Technische Hochschule, CH-8093, Zürich, Switzerland

关键词: Cyanobacteria;    Calothrix;    Phycobilisome;    Phycoerythrin;    Linker polypeptide;    Amino acid sequence;    Chromatic adaptation;   

DOI  :  10.1016/0014-5793(92)80318-B

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Microanalyses by SDS-PAGE and microsequencing demonstrate that, under green-light conditions, 3 C-phycoerythrin associated rod-linker polypeptides with different N-terminal amino acid sequences are present in phycobilisomes (PBS) from Calothrix sp. 7601 cells. Two of these polypeptides, corresponding to SDS-PAGE bands at 36 and 37 kDa, could be assigned, respectively, to the cpeC and epeD genes found on a separate cpeCD-operon in Calothrix sp. 7601 (Federspiel, N.A. and Grossman, A.R. (1990) J. Bacteriol. 172, 4072-4081). The third C-PE rod-linker polypeptide, L_R,2 ^PE,33, requires, therefore, a third gene with the suggested locus designation ‘cpeE’. A C-PE (αβ)₆-L_R,2 ^PE,33 complex containing this third rod-linker polypeptide could be isolated from phycobilisomes and characterized. PBS from both green- and red-light cells of Calothrix contain a single, unique L_RC ²⁸ rod-core linker polypeptide which is not altered during chromatic adaptation.

【 授权许可】

Unknown