Phytochromes: molecular structure, photoreceptor process and physiological function

Sineshchekov, V.A.

doi:10.1007/978-94-011-4832-0_25

Cited by 10 publications

(12 citation statements)

References 135 publications

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“…These results lead us to the following major conclusions: first, the fact that phyA/P⌽B possesses the properties of phyAЉ (␥ 1 Ͻ 0.1) suggests that the differences between phyAЉ and phyAЈ are not connected with the integrity of the molecule and confirms that both phyAЈ and phyAЉ are fulllength phytochromes encoded by the PHYA gene. Second, the considerable spectroscopic differences between phyAЈ and phyA/P⌽B imply some sort of plant-specific effects (posttranslational modifications, molecular interactions, localization), as was suggested earlier (3)(4)(5). As these effects are absent in yeast it appears that most of the endogenous phyA in etiolated seedlings (major phyAЈ) in the plant cell is modified by this method.…”

Section: Phototransformation Of Prmentioning

confidence: 64%

“…Method and instruments. The method of in situ low-temperature fluorescence and photochemical investigations of phytochrome used in this work was developed and described in detail (3)(4)(5)(6)(7)(8)(9)(10)(11). In brief, fluorescence emission spectra were recorded at low temperature (85 K) with a laboratory-designed spectrofluorimeter containing two double-grating monochromators (slit width, 2 nm), DFS-12 with a 500 W Xenon lamp as an excitation source and DFS-24 as an analyzing monochromator.…”

Section: Expression Of Phytochromes In Yeastmentioning

confidence: 99%

“…Two phyA pools (subpopulations), phyAЈ and phyAЉ, were detected in the plant cell differing in their spectroscopic and photochemical properties, their abundance and localization pattern in plant tissues and their light stability. Even within phyAЈ different subspecies (most probably conformers of the chromophore) were distinguished (3)(4)(5).…”

Section: Introductionmentioning

confidence: 99%

“…In situ fluorescence measurements of transgenic tobacco overexpressing full-length oat phyA and its C-terminal (⌬786-1129) and N-terminal (⌬7-69) deletion mutants suggested that the 6 kDa N-terminal domain is connected with the spectroscopic and photochemical differences between phyAЈ and phyAЉ (11). It was proposed that the phyA pools probably differ by posttranslational modification and that phyAЉ could be bound to other cellular components (3)(4)(5)12).…”

Section: Introductionmentioning

confidence: 99%

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Recombinant Phytochrome A in Yeast Differs by its Spectroscopic and Photochemical Properties from the Major phyA′ and is Close to the Minor phyA″: Evidence for Posttranslational Modification of the Pigment in Plants¶

Sineshchekov

Hennig

Lamparter

et al. 2001

Photochem Photobiol

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Previously, two pools of phytochrome A (phyA' and phyA") have been detected by in situ low-temperature fluorescence spectroscopy and photochemistry; it was suggested that they might differ in the nature of their posttranslational modification. In order to verify this possibility Arabidopsis and rice (Oryza) phyA were expressed in yeast and the pigments were assembled in vivo with phycocyanobilin (PCB) and phytochromobilin (P phi B). The resulting recombinant phytochromes in the red-light-absorbing form (Pr) were characterized in the yeast cell by (1) the fluorescence emission spectra; (2) the temperature dependence of Pr fluorescence intensity and activation energy of fluorescence decay; and (3) the extent of photoconversion of Pr into photoproduct lumi-R (gamma 1) or far-red-light absorbing form (Pfr) (gamma 2). Both Arabidopsis phyA/PCB and Oryza phyA/P phi B had low gamma 1 of ca 0.05, allowing their attribution to the Pr" phenomenological type of phytochrome comprising phyA", phyB and cryptogam phytochromes. The spectroscopic properties of Oryza phyA/P phi B were also very close to phyA". However, both investigated holoproteins differed from phyA", both with respect to the character of temperature dependence of the fluorescence yield and activation energy. Thus, recombinant Oryza phyA/P phi B is similar but not identical to phyA". The data demonstrate that the low-abundance-fraction plant phyA (phyA") comes from the same gene as the major (phyA') fraction. Because both endogenous phyA fractions differ from the phytochrome expressed in yeast, they appear to be posttranslationally modified and/or bound to partner proteins or cellular substructures. However, the character of the presumed chemical modification is different in phyA' and phyA" and its extent is more profound in the case of the former.

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Section: Phototransformation Of Prmentioning

confidence: 64%

Section: Expression Of Phytochromes In Yeastmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Recombinant Phytochrome A in Yeast Differs by its Spectroscopic and Photochemical Properties from the Major phyA′ and is Close to the Minor phyA″: Evidence for Posttranslational Modification of the Pigment in Plants¶

Sineshchekov

Hennig

Lamparter

et al. 2001

Photochem Photobiol

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“…In situ low‐temperature fluorescence investigations of phytochrome mutants and transgenic plants have shown, however, that the phytochrome system may have further levels of complexity – post‐translationally modified phytochrome states (second level) and conformers of the chromophore within one phytochrome molecular type (third level) (see reviews by Sineshchekov 1995a, 1998, 1999). Two phenomenological phytochrome types were detected in plants differing in spectroscopic and photochemical properties of their Pr form.…”

Section: Introductionmentioning

confidence: 99%

Fluorescence and photochemical properties of phytochromes in wild‐type wheat and a transgenic line overexpressing an oat phytochrome A (PHYA) gene: functional implications

Sineshchekov¹,

Koppel²,

Shlumukov³

et al. 2001

Plant Cell & Environment

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Etiolated seedlings of wild-type wheat and a transgenic line overexpressing an oat PHYA gene were investigated by the use of in situ low-temperature fluorescence spectroscopy. The red-absorbing phytochrome form, Pr, was characterized by (1) fluorescence emission spectrum; (2) total phytochrome content, and (3) by the extent of the Pr → → → → lumi-R photoconversion at low temperature ( γ γ γ γ 1 ), and of the Pr → → → → Pfr photoconversion at ambient temperature ( γ γ γ γ 2 ) as derived from emission data. All the characteristics were shown to be variable and to depend on (1) organ and tissue used; (2) seedling age; (3) transgenic wheat modification, and (

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Polymorphism of Phytochrome A and Its Functional Implications

Sineshchekov

2005

Light Sensing in Plants

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Phytochromes: molecular structure, photoreceptor process and physiological function

Cited by 10 publications

References 135 publications

Recombinant Phytochrome A in Yeast Differs by its Spectroscopic and Photochemical Properties from the Major phyA′ and is Close to the Minor phyA″: Evidence for Posttranslational Modification of the Pigment in Plants¶

Recombinant Phytochrome A in Yeast Differs by its Spectroscopic and Photochemical Properties from the Major phyA′ and is Close to the Minor phyA″: Evidence for Posttranslational Modification of the Pigment in Plants¶

Fluorescence and photochemical properties of phytochromes in wild‐type wheat and a transgenic line overexpressing an oat phytochrome A (PHYA) gene: functional implications

Polymorphism of Phytochrome A and Its Functional Implications

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