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The 8 linker-polypeptides from the cyanobacterium Mastigocladus laminosus were examinedby comparative amino-acid sequence analysis for the predicted domain structure reported in the literatur(Glauser 1991, Esteban 1993) in detail using split sequences for the rod, rod-core and for the repeats fromthe core-membrane linker-polypeptide (Lcm127.6). This analysis gives two distinct domains, where domain1 (∼ 22 kDa, identity between 31 and 70%) is present in the N-terminal two thirds of the class II linkers(∼ 30 kDa) and in the repeats of the Lcm127.6, and domain 2 (∼ 10 kDa, identity between 28 and 41%) inthe C-terminal part of the class II rod linkers (Lr31.5 and Lr32.5) and in the two capping linkers (Lc7.7 and Lr8.2). Based on these data, X-ray structure analysis from phycobiliproteins and proteolysis experiments, aninterlocking model for the phycobilisome rod organization is proposed, with linkers protruding from onephycobilisome disk into the neighbouring one

international journal of photoenergy

Model for the phycobilisome rod with interlocking disks based on domain-weighted linker-polypeptide sequence homologies of<i>Mastigocladus laminosus</i>

Model for the phycobilisome rod with interlocking disks based on domain-weighted linker-polypeptide sequence homologies ofMastigocladus laminosus