Abstract
The 8 linker-polypeptides from the cyanobacterium Mastigocladus laminosus were examined by 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 from the core-membrane linker-polypeptide (L-cm (127.6)). This analysis gives two distinct domains, where domain 1 (similar to 22 kDa, identity between 31 and 70%) is present in the N-terminal two thirds of the class II linkers (similar to 30 kDa) and in the repeats of the Lcm 127.6, and domain 2 (similar to 10 kDa, identity between 28 and 41%) in the C-terminal part of the class II rod linkers (L-r(31.5) and L-r(32.5)) and in the two capping linkers (L-c(7.7) and L-r(8.2)). Based on these data, X-ray structure analysis from phycobiliproteins and proteolysis experiments, an interlocking model for the phycobilisome rod organization is proposed, with linkers protruding from one phycobilisome disk into the neighbouring one.
Dokumententyp: | Zeitschriftenartikel |
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Publikationsform: | Publisher's Version |
Fakultät: | Biologie |
Themengebiete: | 500 Naturwissenschaften und Mathematik > 570 Biowissenschaften; Biologie
500 Naturwissenschaften und Mathematik > 580 Pflanzen (Botanik) |
URN: | urn:nbn:de:bvb:19-epub-24379-8 |
ISSN: | 1110-662X |
Sprache: | Englisch |
Dokumenten ID: | 24379 |
Datum der Veröffentlichung auf Open Access LMU: | 26. Mrz. 2015, 15:45 |
Letzte Änderungen: | 04. Nov. 2020, 13:06 |