ORIGIN OF THE RED SHIFTED ABSORPTION IN PHYCOCYANIN 632 FROM <i>Mastigocladus laminosus</i>

Gottschalk, L.; Fischer, Richard W.; Lottspeich, Friedrich; Scheer, Hugo

doi:10.1111/j.1751-1097.1991.tb02017.x

Cited by 22 publications

(16 citation statements)

References 23 publications

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“…associated PC have been well characterized in previous studies [42][43][44] and are distinct from that of trimeric PC. Rods have an absorption maximum at 629-638 nm, red shifted compared to that of trimeric PC whose maximum is at 621 nm, 4,45 and this was confirmed in the rods isolated here, with an absorption maximum at 635 nm (Fig. 3a).…”

Section: Isolation Characterization and Crystallization Of Pc Rod Ssupporting

confidence: 79%

“…There is actually little clear-cut evidence for this suggestion, 2,9,45,57 but it is clear that in mutants lacking a specific linker, the appropriate substructure (rod or core) does not assemble correctly. In all electron microscopy studies published, The α and β subunits are depicted in yellow and blue helical tubes, respectively, with the two monomers removed for clarity.…”

Section: Model For Linker Association With Rods and Coresmentioning

confidence: 89%

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High-Resolution Crystal Structures of Trimeric and Rod Phycocyanin

David

Marx

Adir

2011

Journal of Molecular Biology

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Section: Isolation Characterization and Crystallization Of Pc Rod Ssupporting

confidence: 79%

Section: Model For Linker Association With Rods and Coresmentioning

confidence: 89%

High-Resolution Crystal Structures of Trimeric and Rod Phycocyanin

David

Marx

Adir

2011

Journal of Molecular Biology

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“…These elements, not present in the absorption spectra of the other allophycocyanin complexes, remained equally present in all AP,,, preparations. However, the possibility of contamination with phycocyanin rod-core complexes, known to absorb precisely in this spectral region (Gottschalk et al, 1991 ;Glauser et al, 1993), could not be excluded.…”

Section: Resultsmentioning

confidence: 99%

Isolation, Characterization and Electron Microscopy Analysis of A Hemidiscoidal Phycobilisome Type from the Cyanobacterium Anabaena sp. PCC 7120

Ducret¹,

Sidler²,

Wehrli³

et al. 1996

European Journal of Biochemistry

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In this work we present the characterization of a hemidiscoidal phycobilisome type of the heterocystforming cyanobacterium Anabuena sp. PCC 7120. The phycobilisome of this organism contains allophycocyanin, phycocyanin and phycoerythrocyanin, similar to the closely related thermophilic cyanobacterium Mastigocladus laminosus. Intact phycobilisomes exhibit an absorption maximum at 619 nm and two fluorescence maxima at 664 nm and 680 nm, corroborating the presence of a complete energy pathway along the antenna. Upon dissociation, the phycobiliproteins were released from the phycobilisome. One phycoerythrocyanin, one phycocyanin and three allophycocyanin complexes were isolated by ion-exchange chromatography and characterized by absorption and fluorescenc'e spectroscopy and by SDS/ PAGE. The polypeptides contained in the phycobilisome of Anabuena sp. PCC 7120 were subjected to SDSPAGE, blotted onto poly(viny1idendifluoride) membranes and identified by amino-terminal sequence analysis. The amino-terminal sequences of the polypeptides belonging to the phycoerythrocyanin and phycocyanin families were identical with the derived sequences of their corresponding genes. Partial amino-terminal sequences of the polypeptides belonging to the allophycocyanin family are presented here. Our results show that the phycobiliproteins and linker polypeptides from Anabnenn sp. PCC 7120 are similar to the phycobilisome components characterized in other cyanobacteria.The phycobilisome of Anabaena sp. PCC 7120 was extensively analyzed by electron microscopy. It differs from the common hemidiscoidal tricylindrical, six-rod phycobilisome type by a core domain consisting of five core cylinders surrounded by up to eight rods radiating in a hemidiscoidal manner. One rod is linked to each basal core cylinder, whereas the remaining core cylinders bind two rods each. On the basis of the data presented in this work, a revised model for the hemidiscoidal pentacylindrical phycobilisome of Anabaena sp. PCC 7120, M. lnminosus and Anubaenu variabilis is proposed. This model accounts more accurately for the 'grape' pattern typically exhibite'd by these phycobilisomes in electron micrographs.Keywords: phycobilisome ; phycobiliprotein ; electron microscopy ; cyanobacterium ; photosynthesis.The major light-harvesting complex in cyanobacteria and red algae is the phycobilisome, a macromolecular complex that is attached to the surface of the photosynthetic membranes (for reviews, see Bryant,

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“…Also, the linker proteins interact either directly or indirectly with the chromophores causing changes in their environment. These changes can modulate the spectral properties of different phycobilisome subassemblies (Gottschalk et al 1991(Gottschalk et al , 1993Reuter et al 1999). The rod linker proteins of G. violaceus, CpcC1, CpcC2, CpeC, CpeD and CpeE, have been identified by N-terminal sequencing (Gutié rrez-Cirlos et al 2006).…”

Section: Introductionmentioning

confidence: 99%

The presence of multidomain linkers determines the bundle-shape structure of the phycobilisome of the cyanobacterium Gloeobacter violaceus PCC 7421

et al. 2007

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The complete genome sequence of Gloeobacter violaceus [Nakamura et al. (2003a, b) DNA Res 10: [37][38][39][40][41][42][43][44][45] allows us to understand better the structure of the phycobilisomes (PBS) of this cyanobacterium. Genomic analysis revealed peculiarities in these PBS: the presence of genes for two multidomain linker proteins, a core membrane linker with four repetitive sequences (REP domains), the absence of rod core linkers, two sets of phycocyanin (PC) a and b subunits, two copies of a rod PC associated linker (CpcC), and two rod cap associated linkers (CpcD). Also, there is one ferredoxin-NADP + oxidoreductase with only two domains. The PBS proteins were investigated by gel electrophoresis, amino acid sequencing and peptide mass fingerprinting (PMF). The two unique multidomain linkers contain three REP domains with high similarity and these were found to be in tandem and were separated by dissimilar Arms. One of these, with a mass of 81 kDa, is found in heavy PBS fragments rich in PC. We propose that it links six PC hexamers in two parallel rows in the rods. The other unique linker has a mass of 91 kDa and is easily released from the heavy fragments of PBS. We propose that this links the rods to the core. The presence of these multidomain linkers could explain the bundle shaped rods of the PBS. The presence of 4 REP domains in the core membrane linker protein (129 kDa) was established by PMF. This core linker may hold together 16 AP trimers of the pentacylindrical core, or alternatively, a tetracylindrical core of the PBS of G. violaceus.

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ORIGIN OF THE RED SHIFTED ABSORPTION IN PHYCOCYANIN 632 FROM Mastigocladus laminosus

Cited by 22 publications

References 23 publications

High-Resolution Crystal Structures of Trimeric and Rod Phycocyanin

High-Resolution Crystal Structures of Trimeric and Rod Phycocyanin

Isolation, Characterization and Electron Microscopy Analysis of A Hemidiscoidal Phycobilisome Type from the Cyanobacterium Anabaena sp. PCC 7120

The presence of multidomain linkers determines the bundle-shape structure of the phycobilisome of the cyanobacterium Gloeobacter violaceus PCC 7421

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