Picosecond time-resolved energy transfer in Porphyridium cruentum. Part I. In the intact alga

Porter, George; Tredwell, C.J.; Searle, G.F.W.; Barber, James

doi:10.1016/0005-2728(78)90029-4

Cited by 186 publications

(65 citation statements)

References 16 publications

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“…During the gradual association of phycobilisomes, this trans fer chain is extended successively to yield "Forster-cascades" Due to their architecture, each pair of neighboring pigments provides for an optimal overlap of the emission band of the donor and the absorption band of the acceptor (Table 4). This process was demonstrated for biliproteins with different chromophores 1140 ' 142,2971 , of heteroaggregates 1223 253J , and of whole phycobilisomes 1143,289,2901 . In the intact phyco bilisome, the result of this process is such, that the chromo- According to the data summarized above, the morphology of the antennas and the structure of the biliproteins would seem to be closely related.…”

Section: Phycobiliproteinsmentioning

confidence: 87%

Biliproteins

Scheer¹

1981

Angew. Chem. Int. Ed. Engl.

151

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Section: Phycobiliproteinsmentioning

confidence: 87%

Biliproteins

Scheer¹

1981

Angew. Chem. Int. Ed. Engl.

151

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“…The phycobilisome, the major light harvesting complex of eukaryotic red algae and procaryotic cyanobacteria (16, 18- (43). The interactions of the biliproteins with the nonpigmented linker polypeptides (47) cause minor shifts in the spectral properties of the associated chromophores and may increase the efficiency of energy transfer between hexamers (18)(19)(20).…”

Section: Abstracrmentioning

confidence: 99%

Changes in Accumulation and Synthesis of Transcripts Encoding Phycobilisome Components during Acclimation of Fremyella diplosiphon to Different Light Qualities

Oelmüller

Conley²,

Federspiel³

et al. 1988

Plant Physiol.

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“…The predominant cyanobacterial light-harvesting complexes, called phycobilisomes, are multiprotein structures located on the surface of the photosynthetic membranes (19,20). The phycobilisome is a very effective antenna complex, harvesting light in the 500-to 650-nm range and transferring this energy to chlorophyll at better than 95% efficiency (34). The transfer of light energy through the phycobilisome is mediated by a network of bilin chromophores that are covalently attached to the major phycobilisome structural components, the biliproteins.…”

mentioning

confidence: 99%

Genes for phycocyanin subunits in Synechocystis sp. strain PCC 6701 and assembly mutant UV16

Anderson

Grossman

1990

J Bacteriol

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The cyanobacterial phycobilisome is a large protein complex located on the photosynthetic membrane. It harvests light energy and transfers it to chlorophyll for use in photosynthesis. Phycobilisome assembly mutants in the unicellular cyanobacterium Synechocystis sp. strain 6701 have been characterized. One such mutant, UV16, contains a defect in the assembly of the biliprotein phycocyanin. We report the cloning and sequencing of the phycocyanin genes from wild-type Synechocystis strain 6701 and demonstrate an alteration in the gene for the phycocyanin a subunit in UV16. Possible consequences of the lesion on phycobilisome assembly were assessed from its position in the phycocyanin tertiary and quaternary structures. The UV16 phenotype is complex and includes a reduced level of phycocyanin relative to that in the wild type. To determine whether the lower phycocyanin content results from lower transcript levels, a fragment of cpcBA was used as a probe for quantitating phycocyanin mRNA. Both the wild type and UV16 contained two phycocyanin transcripts of approximately 1.4 and 1.5 kilobases that were equal in abundance and that did not vary with light quality during cell growth. Equal levels of these transcripts in the wild type and UV16 suggest that the lower phycocyanin content in the mutant may be due to posttranscriptional events. The 5' ends of the two phycocyanin mRNAs were mapped at 100 and 223 base pairs upstream of the cpcB initiation codon. Homologous regions upstream of the putative transcription initiation sites may be important for maintaining high levels of transcription from the Synechocystis strain 6701 phycocyanin gene set.

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Picosecond time-resolved energy transfer in Porphyridium cruentum. Part I. In the intact alga

Cited by 186 publications

References 16 publications

Biliproteins

Biliproteins

Changes in Accumulation and Synthesis of Transcripts Encoding Phycobilisome Components during Acclimation of Fremyella diplosiphon to Different Light Qualities

Genes for phycocyanin subunits in Synechocystis sp. strain PCC 6701 and assembly mutant UV16

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