Molecular assembly of the phycobilisomes from the cyanobacterium Mastigocladus laminosus

Reuter, W; Nickel-Reuter, Claudia

doi:10.1016/1011-1344(93)80040-g

Cited by 32 publications

(38 citation statements)

References 57 publications

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“…The phycocyanin trimers of both strains turned out to be unstable during the separation. This contrasts with preparations of high-molecular-weight phycocyanin complexes from other cyanobacteria and strains of the Rhodophyceae (30)(31)(32)(33)(34). The disintegration of trimers into mono-and dimeric subcomplexes in strains BO 8402 and BO 9201 seems to be independent of the pH value or the buffer system but is delayed by high buffer and sucrose molarities.…”

Section: Resultsmentioning

confidence: 90%

“…2b). Such an absorbance behavior is typical for highly organized sequentially assembled phycocyanin complexes (32 (Fig. 4) Electron-microscopical investigations of the isolated biliprotein complexes.…”

Section: Resultsmentioning

confidence: 99%

“…The biliproteins are joined by different linker polypeptides LRX that facilitate the sequential assembly and determine the different spectral properties of the subcomplexes (21). The substructure of the rods was postulated to be exclusively hexameric ((X)6 -LRX (19), but recent results indicate a partial assembly of trimeric biliprotein complexes forming hexameric stacks (32). The core is built up by a bi-or tricylindrical central pigment-linker complex, APCM, comprising allophycocyanin and two copies of the anchor polypeptide LCM.…”

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confidence: 99%

“…It serves as backbone of the phycobilisome and as a structural bridge to photosystem 11 (10,34,35 (33,34). However, the peripheral trimeric allophycocyanin complexes seem not essential for phycobilisome assembly (25,32). Energy is transferred from the outer chromophores of the rods to the terminal acceptors of the allophycocyanin core, allophycocyanin B and LCM (21).…”

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confidence: 99%

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Structure, composition, and assembly of paracrystalline phycobiliproteins in Synechocystis sp. strain BO 8402 and of phycobilisomes in the derivative strain BO 9201

et al. 1994

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The phycobiliproteins of the unicellular cyanobacterium Synechocystis sp. strain BO 8402 and its derivative strain BO 9201 are compared. The biliproteins of strain BO 8402 are organized in paracrystalline inclusion bodies showing an intense autofluorescence in vivo. These protein-pigment aggregates have been isolated. The highly purified complexes contain phycocyanin with traces of phycoerythrin, corresponding linker polypeptides LR3PC and LR3PE (the latter in a small amount), and a unique colored polypeptide with an Mr of 55,000, designated L55. Allophycocyanin and the core linker polypeptides are absent. The substructure of the aggregates has been studied by electron microscopy. Physiological and genetic implications of the unusual pigment compositions of both strains are discussed.Phycobiliproteins are the major light-harvesting antennae of cyanobacteria and members of the families Rhodophyceae and Cryptophyceae (36,41). In cyanobacteria and members of the Rhodophyceae, they are assembled in phycobilisomeshigh-molecular-weight protein-pigment complexes with Mrs ranging from 5,000,000 to 20,000,000 (20). Phycobilisomes are connected with dimeric or tetrameric photosystem II complexes and localized along with rows of photosystem II particles at the protoplasmic surface of the thylakoid membranes (16,24). They have been characterized in numerous electronmicroscopical (28), spectroscopical (23), biochemical (19-22), genetic (8), and physiological (22, 39, 40) studies. Phycobilisomes consist of a core from which radiate 6 to 10 rods in a specific assembly classified as bundle shaped, hemidiscoidal, or hemiellipsoidal (21,42,44). The rods comprise either only phycocyanin or, in addition, phycoerythrin and, in some cases, phycoerythrocyanin (7), in ratios determined by genetic and environmental parameters (40). The biliproteins are joined by different linker polypeptides LRX that facilitate the sequential assembly and determine the different spectral properties of the subcomplexes (21). The substructure of the rods was postulated to be exclusively hexameric ((X)6 -LRX (19), but recent results indicate a partial assembly of trimeric biliprotein complexes forming hexameric stacks (32). The core is built up by a bi-or tricylindrical central pigment-linker complex, APCM, comprising allophycocyanin and two copies of the anchor polypeptide LCM. It serves as backbone of the phycobilisome and as a structural bridge to photosystem 11 (10,34,35 (33,34). However, the peripheral trimeric allophycocyanin complexes seem not essential for phycobilisome assembly (25,32). Energy is transferred from the outer chromophores of the rods to the terminal acceptors of the allophycocyanin core, allophycocyanin B and LCM (21). Further energy transmission to photosystem II is influenced by environmental factors (30, 40) and state transition processes (4).Synechocystis sp. strain BO 8402 was isolated from the prealpine Lake Constance (12). The strain is characterized by an intense red autofluorescence originating from a localized area within...

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Section: Resultsmentioning

confidence: 90%

Section: Resultsmentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

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Structure, composition, and assembly of paracrystalline phycobiliproteins in Synechocystis sp. strain BO 8402 and of phycobilisomes in the derivative strain BO 9201

et al. 1994

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“…It was previously demonstrated (31,33) that linker proteins could be degraded in vitro within isolated PBS by some coisolated proteolytic enzyme(s). Here we confirmed this observation: there was a selective loss of L R 33 and L CM 99 linker proteins in PBS isolated from the wild type when incubated at 37°C for 3 h. However, this linker degradation was no longer observed when using PBS isolated from ⌬sppA1.…”

Section: Discussionmentioning

confidence: 99%

Involvement of the SppA1 Peptidase in Acclimation to Saturating Light Intensities in Synechocystis sp. Strain PCC 6803

et al. 2004

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The sll1703 gene, encoding an Arabidopsis homologue of the thylakoid membrane-associated SppA peptidase, was inactivated by interposon mutagenesis in Synechocystis sp. strain PCC 6803. Upon acclimation from a light intensity of 50 to 150 E m ؊2 s ؊1 , the mutant preserved most of its phycobilisome content, whereas the wild-type strain developed a bleaching phenotype due to the loss of about 40% of its phycobiliproteins. Using in vivo and in vitro experiments, we demonstrate that the ⌬sppA1 strain does not undergo the cleavage of the L R 33 and L CM 99 linker proteins that develops in the wild type exposed to increasing light intensities. We conclude that a major contribution to light acclimation under a moderate light regime in cyanobacteria originates from an SppA1-mediated cleavage of phycobilisome linker proteins. Together with changes in gene expression of the major phycobiliproteins, it contributes an additional mechanism aimed at reducing the content in phycobilisome antennae upon acclimation to a higher light intensity.

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Allophycocyanin 1 as a Near-Infrared Fluorescent Tracer: Isolation, Characterization, Chemical Modification, and Use in a Homogeneous Fluorescence Resonance Energy Transfer System

Trinquet¹,

Maurin²,

Préaudat³

et al. 2001

Analytical Biochemistry

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Molecular assembly of the phycobilisomes from the cyanobacterium Mastigocladus laminosus

Cited by 32 publications

References 57 publications

Structure, composition, and assembly of paracrystalline phycobiliproteins in Synechocystis sp. strain BO 8402 and of phycobilisomes in the derivative strain BO 9201

Structure, composition, and assembly of paracrystalline phycobiliproteins in Synechocystis sp. strain BO 8402 and of phycobilisomes in the derivative strain BO 9201

Involvement of the SppA1 Peptidase in Acclimation to Saturating Light Intensities in Synechocystis sp. Strain PCC 6803

Allophycocyanin 1 as a Near-Infrared Fluorescent Tracer: Isolation, Characterization, Chemical Modification, and Use in a Homogeneous Fluorescence Resonance Energy Transfer System

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