Phycobilisome structure in the cyanobacteria Mastigocladus laminosus and Anabaena sp. PCC 7120

Manuel GLAUSER, Donald A. BRYANT, Gerhard FRANK, Ernst WEHRLI, S. Sandro RUSCONI, Walter SIDLER, Herbert ZUBER

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72 Scopus citations


Phycobilisomes of the cyanobacteria Mastigocladus laminosus and Anabaena sp. PCC7120 differ from typical tricylindrical, hemidiscoidal phycobilisomes in three respects. Firstly, size comparisons of the core‐membrane linker phycobiliproteins (LCM)in different cyanobactertia by SDS/PAGE reveal an apparent molecular mass of 120 kDa for the LCM of M. laminusus and Anabaena sp. PCC7120. This observation suggests that the polypeptides of these species have four linker‐repeat domains. Secondly, phycobilisomes of M. laminosus are shown to contain at least three, but most probably four, different rod‐core linker polypeptides (LRC). These LRC, which attach the peripheral rods to the core and thereby make phycocyanin/allophycocyanin contacts, have been identified and characterized by N‐terminal amino acid sequence analysis. Additionally, electron microscopy of phycobilisomes isolated from M. laminosus and Anabaena sp. PCC7120 reveals similar structures which differ from those of Calorthrix sp. PCC7601 with their typical six, peripheral rods. Based upon protein‐analytical results and a reinterpretation of the data of [Isono, T. & Katoh, T. (1987) Arch. Biochem. Biophys. 256, 317–324], we discuss structural implications of recent findings on the established hemidiscoidal model for the phycobilisomes of M. laminosus and Anabaena sp. PCC7120. Up to eight peripheral rods are suggested to radiate from a modified core substructure which contains two additional peripheral allophycocyanin hexamer equivalents that serve as the core‐proximal discs for two peripheral rods.

Original languageEnglish (US)
Pages (from-to)907-915
Number of pages9
JournalEuropean Journal of Biochemistry
Issue number3
StatePublished - May 1992

All Science Journal Classification (ASJC) codes

  • Biochemistry


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