Phycoerythrins of the Red Alga <i>Callithamnion</i>

Yu, Myeong-Hee; Glazer, Alexander N.; Spencer, Ken G.; West, John A.

doi:10.1104/pp.68.2.482

Cited by 74 publications

(25 citation statements)

References 28 publications

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“…5, Table II). The PE of Gracilaria is quite similar to the R-PEs from the macrophytic red algae Ceramium, Grifithsia, and Callithamnion (8,19,30 (29,30), accounted for less than 10% of the total PE and was not purified. The unusually deep trough at 51 1 nm ofan aqueous extract of obr (Fig.…”

Section: Resultsmentioning

confidence: 98%

“…One nuclear mutant examined, obr, synthesizes a PE which is spectroscopically altered though similar to naturally occurring PE from other red algal species (3,13,28,30). The molar ratios of phycoerythrobilin to phycourobilin in wild type and obr RPEs is 4.2 and 2.6, respectively; therefore, obr can synthesize phycoerythrobilin, yet its PE is deficient in this chromophore.…”

Section: Principalmentioning

confidence: 99%

“…The molar ratios of phycoerythrobilin to phycourobilin in wild type and obr RPEs is 4.2 and 2.6, respectively; therefore, obr can synthesize phycoerythrobilin, yet its PE is deficient in this chromophore. Comparable PEs were isolated from two species of Callithamnion and from Callithamnion roseum grown under a range of light intensities (30). The PEs of wild type and obr chromatograph equivalently on hydroxylapatite, the PE content of obr is nearly the same as that of wild type, and the phycobilisomes from these two strains are also equivalent in size and structure (16).…”

Section: Principalmentioning

confidence: 99%

“…The red biliprotein, PE, occurs in many spectral forms and is found in most red algae and in some cyanobacteria. R-PE, the spectral type found in many higher red algae, probably has an (af3)6'y subunit structure (30). R-PE has absorption maxima at 498 nm, assigned to phycourobilin, and at 545 and 565 nm, assigned to phycoerythrobilin chromophores.…”

mentioning

confidence: 99%

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Light-Harvesting System of the Red Alga Gracilaria tikvahiae

Kursar¹,

Meer²,

Alberte³

1983

Plant Physiol.

146

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ABSTRACIWild type Gracilaria tik'ahiae, a macrophytic red alga, and fourteen genetically characterized pigment mutants were analyzed for their biliprotein and chlorophyll contents. The same three biliproteins, phycoerythrin, phycocyanin, and allophycocyanin, which are found in the wild type are found in all the Mendelian and non-Mendelian mutants examined. Some mutants overproduce R-phycoerythrin while others possess only traces of phycobiliprotein; however, no phycoerythrin minus mutants were found. Two of the mutants are unique; one overproduces phycocyanin relative to allophycocyanin while the nuclear mutant obr synthesizes a phycoerythrin which is spectroscopically distinct from the R-phycoerythrin of the wild type. The phycoerythrin of obr lacks the typical absorption peak at 545 nanometers characteristic of R-phycoerythrin and possesses a phycoerythrobilin to phycourobilin chromophore ratio of 2.6 in contrast to a ratio of 4.2 found in the wild type. Such a lesion provides evidence for the role of nuclear genes in phycoerythrin synthesis. In addition, comparisons are made of the pigment compositions of the Gracilaria strains with those of Neoagardhiella bailyei, a macrophytic red alga which has a high phycoerythrin content, and Anacystis nidulans, a cyanobacterium which lacks phycoerythrin. The mutants described here should prove useful in the study of the genetic control of phycobiliprotein synthesis and phycobilisome structure and assembly.The functional photosynthetic unit of 02-evolving plants is composed of large arrays of light-harvesting pigment-proteins which are associated with the reaction centers and electron transport chains of PSI and PSII. While the reaction centers, electron transport chains, and dark reactions of photosynthesis are probably very similar in the major plant groups, the lightharvesting systems are quite diverse. For example, the antennae pigments fucoxanthin and Chl c are found in the photosynthetic unit of the diatoms and brown algae. In the red algae, Cryptomonads, and cyanobacteria, the phycobiliproteins serve this function while Chl b functions in the green plants (22). These pigments along with the proteins which bind them are major '

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Section: Resultsmentioning

confidence: 98%

Section: Principalmentioning

confidence: 99%

Section: Principalmentioning

confidence: 99%

mentioning

confidence: 99%

See 2 more Smart Citations

Light-Harvesting System of the Red Alga Gracilaria tikvahiae

Kursar¹,

Meer²,

Alberte³

1983

Plant Physiol.

146

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“…Even members of other Ceramiaceae genera examined (Antithamnion, Seirospora and Griffithsia, results not shown) had the typical three-peaked R-phycoerythrin. Examination of the molecular basis of the spectroscopic difference between the phycoerythrin of the Massachusetts C. roseum and those of the other Callithamnion species is the subject of a separate report (Yu et al, 1981).…”

Section: Phycoerythrinmentioning

confidence: 99%

Phycoerythrin and interfertility patterns inCallithamnion(Rhodophyta) isolates

Spencer

West

et al. 1981

British Phycological Journal

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Bilin Metabolism in Plants: Structure, Function and Haem Oxygenase Regulation of Bilin Biosynthesis

Shekhawat

Parihar

Mahawar

et al. 2019

Encyclopedia of Life Sciences

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Bilins are open‐chain tetrapyrroles with a wide range of visible and nearly visible‐light absorption and emission properties. The linear tetrapyrrole molecules function as chromophores of the light‐harvesting phycobiliproteins and phytochrome‐mediated light sensing in photosynthetic organisms. They are derived from the cyclic precursor haem. The initial step in bilin biosynthesis is the conversion of haem into biliverdin (BV IX α) catalysed by haem oxygenase, which is subsequently reduced to specific bilins by ferredoxin‐dependent bilin reductases (FDBRs). Bilins usually bound to apoproteins via single or double covalent bonds to form a macromolecular complex phycobilisomes. The attachment of apoproteins to bilin is an autocatalytic process, but bilin lyases are required for the specific attachment of bilin chromophores to phycobiliprotein apoproteins. Besides the biosynthesis, structure and functions of bilins, this article also aims to recapitulate and discuss the current progress in the field of bilins and to emphasise the emerging areas. Key Concepts Bilins are open‐chain tetrapyrrole non‐metallic colour compounds formed as a metabolic product of protoporphyrin IX. Biliverdin IX α is the common precursor of all naturally occurring bilins. Haem oxygenase (HO) and ferredoxin‐dependent bilin reductases (FDBRs) are the two key enzymes involved in the biosynthesis of bilins. Phycobiliproteins assemble with bilins to form phycobilisomes, which help in light harvesting and energy transfer. Bilin plays a significant role in various physiological processes, namely, photosynthesis, respiration, light perception, signalling, cell defence against oxidative stress, nitrate and sulfate assimilation and programmed cell death.

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Phycoerythrins of the Red Alga Callithamnion

Cited by 74 publications

References 28 publications

Light-Harvesting System of the Red Alga Gracilaria tikvahiae

Light-Harvesting System of the Red Alga Gracilaria tikvahiae

Phycoerythrin and interfertility patterns inCallithamnion(Rhodophyta) isolates

Bilin Metabolism in Plants: Structure, Function and Haem Oxygenase Regulation of Bilin Biosynthesis

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