Disk-to-Disk Transfer as the Rate-Limiting Step for Energy Flow in Phycobilisomes

Glazer, Alexander N.; Yeh, Sung-Wei; Webb, S. P.; Clark, J. H.

doi:10.1126/science.227.4685.419

Cited by 58 publications

(36 citation statements)

References 23 publications

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“…This finding is in line with the results from other groups (Hanzlik et a/., 1985;Kobayashi et al, 1979) and also with the observation of fast anisotropy decays (Hefferle et al, 1983a,b;Hefferle et al, 1984a.b). Different results have been reported recently for isolated R-phycoerythrin and allophycocyanin (Glazer et al, 1985). Both of these phycobiliproteins have not been studied by us so far, however.…”

Section: Short-lived Fluorescence Componentsmentioning

confidence: 77%

“…1982;Holzwarth et al, 1983b;Suter et al. 1984;Hefferle et al, 1984a;Hefferle et al, 1984b;Gillbro ef ul., 1983;Mimuro et al, 1984;Yamazaki et al, 1984;Switalski and Sauer, 1984;Wong et al, 1981;Holzwarth, 1985;Wehrmeyer et al, 1985;Gillbro et al, 1985;Mimuro et al, 1985;Glazer et al, 1985;Hanzlik et ul., 1985; for recent reviews see Karukstis and Sauer, 1983;Scheer, 1985). These studies support a general scheme, where the excitation energy ~ -.…”

Section: Introdgctionmentioning

confidence: 99%

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Energy Transfer in Trimeric C‐phycocyanin Studied by Picosecond Fluorescence Kinetics

Wendler¹,

John²,

Scheer³

et al. 1986

Photochem & Photobiology

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Abstract-The excited state kinetics of trimeric C-phycocyanin from Masrigocladus /arnirzosu.c. has been measured as a function of the emission and excitation wavelength by the single-photon timing technique with picosecond resolution and simultaneous data analysis. A last decay componcnt of 22 ps (C-phycocyanin with linker peptides) and 36 ps (C-phycocyanin lacking linker peptides) is attributed to efficient energy transfer from sensitizing to fluorcscing chromophores. At long dctcction wavelengths the fast decay components are found to turn into a rise t a m . This finding further corroborates thc concept o f intramolecular energy transfer. Previous reports on the conformational heterogeneity of the chromophores and/or proteins in C-phycocyanin are confirmcd. Our data also provide indications for the importancc of the uncoloured linker peptides for this hctcrogeneity.

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Section: Short-lived Fluorescence Componentsmentioning

confidence: 77%

Section: Introdgctionmentioning

confidence: 99%

Energy Transfer in Trimeric C‐phycocyanin Studied by Picosecond Fluorescence Kinetics

Wendler¹,

John²,

Scheer³

et al. 1986

Photochem & Photobiology

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“…Fluorescence Measurements Steady state fluorescence emission measurements were performed with a Fluorolog 21T22 spectrofluorimeter (Spex Inc., Metuchen, NJ) interfaced with a Digital Equipment 1nc.-based computer system. Timeresolved measurements were obtained using an ultrafast streak camera (6). An optical parametric source gave tunable excitation pulses (7).…”

Section: Crosslinked Allophycocyaninmentioning

confidence: 99%

Fluorescence properties of allophycocyanin and a crosslinked allophycocyanin trimer

Yeh

et al. 1987

Cytometry

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The introduction of phycobiliproteins as fluorescent tags of cells and molecules in 1982 (13) was followed by widespread application of these macromolecules in cell sorting, cell analyses, and immunoassay (5,111. The most commonly used phycobiliproteins are B-and R-phycoerythrins. These proteins have the subunit structure (a/3)Gy with a total molecular weight of -240,000 and contain 34 open chain tetrapyrrole prosthetic groups (bilins) per molecule (3,10,12). Phycoerythrins absorb maximally in the green region of the visible spectrum and emit at 576 nm (2). The (a&y assembly form of phycoerythrin is extremely stable, and no shift in the emission maximum is seen even at 1O-l2M (13).Another phycobiliprotein which has proved valuable as a fluorescent tag is allophycocyanin (AP) (8,9,15). At near neutral pH, this protein exists as a trimer, ( a f i )~, of -100,000 daltons, which contains six bilin prosthetic groups. The trimer has an absorption maximum at 650 nm, an emission maximum at 660 nm, and a quantum yield of -0.4 (2,141. The fact that the excitation and emission maxima for AP lie in the red is particularly important because of the lack of interfering emissions from most biological materials in this region of the spectrum, and because of the ready availability of inexpensive helium-neon lasers. One potential difficulty with AP as a fluorescent tag is that, in contrast to the stability of the phycoerythrins discussed above, AP dissociates at very low concentrations (-1OP8M) to the monomer, a& with a shift in the emission to 645 nm and a decrease in quantum yield. We have recently eliminated this difficulty by preparing a crosslinked AP trimer (XL-AP) which does not dissociate even a t extreme dilution (14). In addition, we have found that XL-AP is markedly more stable at high temperatures than unmodified AP. We anticipate that this AP derivative will be applied widely in cell sorting and analysis. Its properties are such that it may also be well suited as a tag for DNA probes. This report presents data on the wavelength and temperature dependence of the fluorescence of AP and XL-AP. MATERIALS AND METHODS Crosslinked AllophycocyaninAnabaena variabilis AP was purified as previously described (1). To prepare the crosslinked derivative, AP (1.5 mg/ml) in 0.05 M Na-phosphate buffer at pH 7.0 was treated with 35 mM l-ethyl-3-(3-dimethylaminopropy1)carbodiimide (Sigma, St. Louis, MO) for 4 hr at 22°C. The reaction was quenched by the addition of a solution of glycylglycine (Sigma) at pH 7.0 to a final concentration of 0.1 M. The procedure of Ong and Glazer (14) was then used to obtain AP trimer made up of three monoAddress reprint requests to A.N. Glazer,

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“…The balance of the PBS (15%) is composed of linker polypeptides, which are essential for promoting assembly and maintaining the structure of the complex (20,21,32). In addition, linker polypeptides ensure efficient, unidirectional energy transfer from the peripheral pigments to the core and from the core to the chlorophyll of the reaction centers (23,49). The linkers are basic proteins which associate tightly with the acidic biliproteins and range in molecular mass from 8 to 95 kDa.…”

mentioning

confidence: 99%

Isolation and characterization of light-regulated phycobilisome linker polypeptide genes and their transcription as a polycistronic mRNA

Lomax¹,

Conley²,

Schilling³

et al. 1987

J Bacteriol

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Several cyanobacteria adjust both the phycobiliprotein and linker protein composition of the phycobilisome, a light-harvesting complex in cyanobacteria and some eucaryotic algae, to maximize absorption of prevalent wavelengths of light. This process is called complementary chromatic adaptation. We sequenced the amino terminus of a linker polypeptide which is associated with phycocyanin and accumulates to high levels during growth of the cyanobacterium Fremyella diplosiphon in red light. A mixed oligonucleotide encoding a region of this amino terminus was synthesized and used to identify a fragment of F. diplosiphon genomic DNA encoding the linker polypeptide. This linker gene was located between two other linker genes and contiguous to the red-light-induced phycocyanin gene set. Sequences of all three linker genes are presented. These genes were transcribed together onto a large polycistronic mRNA which also encoded the red-light-induced phycocyanin subunits. The relationship of this transcript to the biogenesis of the phycobilisome when F. diplosiphon is grown under different conditions of illumination is discussed.

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Disk-to-Disk Transfer as the Rate-Limiting Step for Energy Flow in Phycobilisomes

Cited by 58 publications

References 23 publications

Energy Transfer in Trimeric C‐phycocyanin Studied by Picosecond Fluorescence Kinetics

Energy Transfer in Trimeric C‐phycocyanin Studied by Picosecond Fluorescence Kinetics

Fluorescence properties of allophycocyanin and a crosslinked allophycocyanin trimer

Isolation and characterization of light-regulated phycobilisome linker polypeptide genes and their transcription as a polycistronic mRNA

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