Core substructure in cyanobacterial phycobilisomes

Gingrich, Jeffrey C.; Lundell, Daniel; Glazer, Alexander N.

doi:10.1002/jcb.240220102

Cited by 57 publications

(28 citation statements)

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“…The late-eluting form showed the phycobiliprotein composition (aAP-Ba$Ppy) and exhibited the same spectral characteristics as the allophycocyanin-B complexes isolated from Synechocystis sp. PCC 6701 (Gingrich et al, 1983) and Synechococcus sp. PCC 6301 (Lundell and Glazer, 1983 b).…”

Section: Discussionmentioning

confidence: 99%

“…The intact complex seems to contain from two to three allophycocyanin-I1 complexes associated with the coremembrane linker polypeptide, similar to complexes isolated from Synechocystis sp. PCC 6701 (Gingrich et al, 1983) and M. laminosus (Reuter and Wehrmeyer, 1990). Unfortunately, the lack of stability of the AP,,,, complex isolated from Anabaena sp.…”

Section: Discussionmentioning

confidence: 99%

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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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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

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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“…The only missing gene is the one which codes for 1318.3, a ,B-type subunit that, like OtAPB and LC92 represents about 3% of the total PB cm'ot3 oftettlP subunit content of the core, i.e., 2 of 72 subunits. On the other hand, the polypeptide content of PBsome cores, as analyzed by two-dimensional gel electrophoresis, revealed the existence of multiple bands for some of the subunits (1,19,22). These results must now be reexamined in relation to the existence of multigene families in Calothrix strain 7601.…”

Section: Discussionmentioning

confidence: 99%

Genes encoding core components of the phycobilisome in the cyanobacterium Calothrix sp. strain PCC 7601: occurrence of a multigene family

et al. 1988

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“…The sodium dodecyl sulfate (SDS) gel system was that of Laemmli (16) with modifications (4). Isoelectric focusing for the first dimension of twodimensional (2-D) gels was performed by the method of O'Farrell and O'Farrell (19) with the ampholine mixture and second-dimension gel of Gingrich et al (10). Molar ratios of biliprotein subunits and linker proteins were estimated by scanning Coomassie-stained SDS gels.…”

Section: Methodsmentioning

confidence: 99%

Mutations that affect structure and assembly of light-harvesting proteins in the cyanobacterium Synechocystis sp. strain 6701

Anderson¹,

Rayner²,

Eiserling³

1987

J Bacteriol

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The unicellular cyanobacterium Synechocystis sp. strain 6701 was mutagenized with UV irradiation and screened for pigment changes that indicated genetic lesions involving the light-harvesting proteins of the phycobilisome. A previous examination of the pigment mutant UV16 showed an assembly defect in the phycocyanin component of the phycobilisome. Mutagenesis of UV16 produced an additional double mutant, UV16-40, with decreased phycoerythrin content. Phycocyanin and phycoerythrin were isolated from UV16-40 and compared with normal biliproteins. The results suggested that the UV16 mutation affected the a subunit of phycocyanin, while the phycoerythrin subunit from UV16-40 had lost one of its three chromophores. Characterization of the unassembled phycobilisome components in these mutants suggests that these strains will be useful for probing in vivo the regulated expression and assembly of phycobilisomes.Phycobilisomes are the light-harvesting structures of cyanobacteria and red algae. Composed of chromophoric biliproteins and nonchromophoric linker proteins, phycobilisomes are organized into two structural domains, the core and the rods (reviewed in reference 12). The core is associated with the thylakoid membrane and contains the allophycocyanin (AP) biliproteins. The rods are attached to the membrane-distal periphery of the core and, in the unicellular cyanobacterium Synechocystis sp. strain 6701, contain phycocyanin (PC) and phycoerythrin (PE) biliproteins and four linker proteins of 27, 30.5, 31.5, and 33.5 kilodaltons (kDa) (9, 12).UV irradiation has been used to obtain pigment mutants in strain 6701 (3). Preliminary characterization of a phycobilisome assembly mutant, UV16, demonstrated intact core substructures with little PC bound and soluble PC trimers that were free of linker proteins. The PE in UV16 assembled into rod substructures that contained the 31.5-and 30.5-kDa PE linker proteins and cosedimented with cores on a sucrose gradient (3). The UV16 strain was mutagenized to find a mutant that would eliminate PE contamination of cores. We obtained the mutant strain UV16-40 from a colony with lighter green pigmentation, indicating decreased PE relative to the parent strain, UV16. We examined relative biliprotein content, assembly of rod components, and the chromatic adaptation response (22) in the UV16 and UV16-40 strains. The defective PC and PE biliproteins were isolated from UV16-40 and compared with normal PC and PE from wildtype (WT) and UV16 strains. The resulting differences suggested the presence of structural lesions in the PC ax subunit of UV16 and the PE ,B subunit of UV16-40. MATERIALS AND METHODSStrains, media, and culture conditions. Synechocystis sp. strain 6701 (Pasteur Culture Collection) and mutant strains were grown in the medium and light conditions described previously (3). Strains UV16 and UV16-40 were obtained after UV mutagenesis (3) tively. The spontaneous reversion frequency for both mutants was not measured directly, but is less than lo-5. To assay chromatic adaptation respo...

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Core substructure in cyanobacterial phycobilisomes

Cited by 57 publications

References 22 publications

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

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

Genes encoding core components of the phycobilisome in the cyanobacterium Calothrix sp. strain PCC 7601: occurrence of a multigene family

Mutations that affect structure and assembly of light-harvesting proteins in the cyanobacterium Synechocystis sp. strain 6701

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