Subunit structure and chromophore composition of rhodophytan phycoerythrins. Porphyridium cruentum B-phycoerythrin and b-phycoerythrin.

Glazer, Alexander N.; Hixson, Craig S.

doi:10.1016/s0021-9258(17)32794-1

Cited by 192 publications

(22 citation statements)

References 36 publications

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“…Here, the molar ratio between PEB and PUB is close to 1 : 1, in view of the fact that in native biliproteins the molar extinction coefficient of PUB is about 1.5-fold bigger than that of PEB. 28,29,34 The autocatalytic isomerization of PEB to PUB has been reported before in one GAF-domain of CBCR from Nostoc punctiforme ATCC 29133. 16 In a R-phycocyanin 34 and phycoerythrin, 35 the isomerization is catalyzed by a lyase.…”

Section: Autocatalytic Chromophorylation Of Gafs With Pebsupporting

confidence: 54%

Orange fluorescent proteins constructed from cyanobacteriochromes chromophorylated with phycoerythrobilin

Sun

Tang

et al. 2014

Photochem Photobiol Sci

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Cyanobacteriochromes are a structurally and spectrally highly diverse class of phytochrome-related photosensory biliproteins. They contain one or more GAF domains that bind phycocyanobilin (PCB) autocatalytically; some of these proteins are also capable of further modifying PCB to phycoviolobilin or rubins. We tested the chromophorylation with the non-photochromic phycoerythrobilin (PEB) of 16 cyanobacteriochrome GAFs from Nostoc sp. PCC 7120, of Slr1393 from Synechocystis sp. PCC 6803, and of Tlr0911 from Thermosynechococcus elongatus BP-1. Nine GAFs could be autocatalytically chromophorylated in vivo/in E. coli with PEB, resulting in highly fluorescent biliproteins with brightness comparable to that of fluorescent proteins like GFP. In several GAFs, PEB was concomitantly converted to phycourobilin (PUB) during binding. This not only shifted the spectra, but also increased the Stokes shift.The chromophorylated GAFs could be oligomerized further by attaching a GCN4 leucine zipper domain, thereby enhancing the absorbance and fluorescence of the complexes. The presence of both PEB and PUB makes these oligomeric GAF-"bundles" interesting models for energy transfer akin to the antenna complexes found in cyanobacterial phycobilisomes. The thermal and photochemical stability and their strong brightness make these constructs promising orange fluorescent biomarkers.

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Section: Autocatalytic Chromophorylation Of Gafs With Pebsupporting

confidence: 54%

Orange fluorescent proteins constructed from cyanobacteriochromes chromophorylated with phycoerythrobilin

Sun

Tang

et al. 2014

Photochem Photobiol Sci

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“…All of these proteins contain a and ß subunits of <20,000 daltons that carry covalently bound bilins (1). Rhodophytan phycoerythrins also contain a y-subunit of 30,000 daltons with attached bilins (9,19). A second type of biliprotein, widely distributed, is the plant photomorphogenetic chromoprotein, phytochrome, a single polypeptide of 120,000 daltons with a single covalently bound bilin (20) .…”

Section: Occurrence Of Biliproteinsmentioning

confidence: 99%

“…The polypeptides purified in this manner showed no absorbance between 350 and 700 nm, and hence we concluded that they did not carry bilin prosthetic groups . However, in a previous study, we had shown that purification of the subunits of the biliprotein b-phycoerythrin under the same conditions led to extensive bleaching of phycoerythrobilin chromophores (9) . Such bleaching was minimized when the purification was performed at spH 3 (9) .…”

mentioning

confidence: 93%

“…However, in a previous study, we had shown that purification of the subunits of the biliprotein b-phycoerythrin under the same conditions led to extensive bleaching of phycoerythrobilin chromophores (9) . Such bleaching was minimized when the purification was performed at spH 3 (9) . In view of these observations, we have developed a rapid isolation procedure for the linker polypeptides in which a strongly acidic pH is maintained throughout.…”

mentioning

confidence: 93%

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A terminal energy acceptor of the phycobilisome: the 75,000-dalton polypeptide of Synechococcus 6301 phycobilisomes--a new biliprotein.

Lundell¹,

Yamanaka²,

Glazer³

1981

The Journal of Cell Biology

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100

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A rapid procedure is described for the isolation of "linker" polypeptides (Lundell, D. ) ., R.C. Williams, and A. N . Glazer. 1981 . /. Biol . Chem. 256:3580-3592) of cyanobacterial phycobilisomes . The 75,000-dalton component of the core of Synechococcus 6301 phycobilisomes isolated b~this procedure has been shown to carry a bilin similar in spectroscopic properties to phycocyanobílin . "Renatured" 75,000-dalton polypeptide has absorption maxima at 610 and 665 nm and a fluorescence emission maximum at 676 nm, similar to that of intact phycobilisomes . A complex of allophycocyanin and a 40,000-dalton bilin-carrying fragment of the 75,000-dalton polypeptide, obtained by limited tryptic digestion, is described. This complex, which lacks allophycocyanin B, shows a fluorescence emission maximum at 676 nm . The above data indicate that the 75,000-dalton polypeptide functions as a terminal energy acceptor in the phycobilisome.

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“…We can see from 9 that the absorbance and fluorescence spectrum of PEB changed with pH. Previous studies have shown that the light absorption spectrum of phycoerythrin depends closely on pH due to structural conformation (Glazer and Hixson 1977;Camara-Artigas et al 2012). Gaigalas et al (2006) determined semiempirically the structure of R-phycoerythrin in the red alga Griffithsia monilis and found that the blue shift effect of the spectrum was caused by the flatness deviation of the conjugated ring A-B.…”

Section: Analysis For Stability Of Absorption and Fluorescence Spectra About Peb With Different Phsmentioning

confidence: 80%

Biosynthesis and preparation of phycoerythrobilin in recombinant Escherichia coli

et al. 2021

J Appl Phycol

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Phycoerythrobilin (PEB) is a special pigment in red algae and cyanobacteria that plays an important role in capturing light energy. As a natural non-toxic pigment with antioxidant properties, PEB is widely used in food and cosmetics industries. At present, the presence of other pigments in red algae and cyanobacteria, such as chlorophyll and phycocyanobilin, makes the preparation of PEB complicated and costly. In this study, the PEB synthesizing enzyme genes of hox1 from Synechocystis sp. PCC6803 and pebS from Nostoc sp. PCC 7120 were co-expressed in Escherichia coli to produce recombinant PEB. In addition, single-factor and response surface methods were used to enhance the yield of recombinant PEB. Under the conditions of lactose concentration at 4 mmol L −1 , induction temperature at 27 °C, OD 600 nm of 0.9, and induction time at 14 h, the concentration of PEB reached 20.37 mg L −1 . In addition, a high-purity (purity > 70%) PEB was obtained through chloroform extraction, and the purified product was verified in UV spectrometry, high-performance liquid chromatography, and mass spectrometry.

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Subunit structure and chromophore composition of rhodophytan phycoerythrins. Porphyridium cruentum B-phycoerythrin and b-phycoerythrin.

Cited by 192 publications

References 36 publications

Orange fluorescent proteins constructed from cyanobacteriochromes chromophorylated with phycoerythrobilin

Orange fluorescent proteins constructed from cyanobacteriochromes chromophorylated with phycoerythrobilin

A terminal energy acceptor of the phycobilisome: the 75,000-dalton polypeptide of Synechococcus 6301 phycobilisomes--a new biliprotein.

Biosynthesis and preparation of phycoerythrobilin in recombinant Escherichia coli

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