Progress in the Molecular Analysis of Phytochrome

Lagarias, J. Clark

doi:10.1111/j.1751-1097.1985.tb01654.x

Cited by 86 publications

(53 citation statements)

References 81 publications

(39 reference statements)

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“…Phytochrome is a chromoprotein existing as a dimer of two 120-kD polypeptides, each with a covalently attached linear tetrapyrrole chromophore (Lagarias, 1985). This pigment undergoes a reversible photo-induced conversion between two distinct forms, a Pr, which is physiologically inactive, Supported in part by a grant from the Intemational Human Frontier Science Program to A.N.…”

mentioning

confidence: 99%

Isolation and Initial Characterization of Arabidopsis Mutants That Are Deficient in Phytochrome A

Nagatani¹,

Reed²,

Chory³

1993

Plant Physiol.

445

400

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Phytochrome, a red/far-red-light photoreceptor protein of plants, is encoded by a small gene family. Phytochrome A (PHYA), the product of the PHYA gene, is the predominant molecular species of phytochrome in etiolated tissue and has been best charaderized biochemically. To define a role for PHYA, we isolated new mutants, designated frel (far-red elongated), in Arabidopsis thaliana that were specifically deficient in PHYA spectral activity and protein accumulation. These mutants were identified on the basis of their long hypocotyl phenotype under continuous far-red light. Although the frel mutants lacked the hypocotyl response to continuous far-red light, their responses to continuous white light and to end-of-day far-red-light treatments were normal. Thus, PHYA appears to play only a minor role in the regulation of hypocotyl elongation under natural conditions. In contrast, the frel mutation affected greening; a frel mutant was less able than the wild type to deetiolate after growth in the dark. However, the potentiation effect of a red-light pulse on accumulation of chlorophyll was not changed significantly in the frel mutants. Thus, the function of PHYA might be highly specialized and restricted to certain phases of Arabidopsis development.

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mentioning

confidence: 99%

Isolation and Initial Characterization of Arabidopsis Mutants That Are Deficient in Phytochrome A

Nagatani¹,

Reed²,

Chory³

1993

Plant Physiol.

445

400

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“…This process alters mutual interactions between the chromophore and the protein, inducing conformational changes in both protein and chromophore (12,13). The involvement of the 6-kDa N-terminal region of the polypeptide in these conformational changes and in the stabilization of the Pfr chromophore is well documented (2,14,15).…”

mentioning

confidence: 99%

In vitro assembly of apophytochrome and apophytochrome deletion mutants expressed in yeast with phycocyanobilin.

Deforce

Tomizawa

Ito

et al. 1991

Proc. Natl. Acad. Sci. U.S.A.

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“…*For correspondence (fax +1 510 559 5678; e-mail quail@mendel.berkeley.edu). (Lagarias, 1985). The phytochrome molecule exists in two spectrally distinct conformations: a R-absorbing form (Pr, ~,max = 666 nm) and a FR-absorbing form (Pfr, Zmax = 730 nm).…”

Section: Introductionmentioning

confidence: 99%

Overexpressed phytochrome C has similar photosensory specificity to phytochrome B but a distinctive capacity to enhance primary leaf expansion

Qin

Kuhn²,

Moran³

et al. 1997

The Plant Journal

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SummaryPhytochrome C (phyC) is a low-abundance member of the five-membered phytochrome family of photoreceptors in Arabidopsis.Towards developing an understanding of the photosensory and physiological functions of phyC, transgenic Arabidopsis plants were generated that overexpress cDNA-encoded phyC and seedling responses to continuous white, red, or far-red light (Wc, Rc or FRc, respectively) were examined. Transgenic seedlings overexpressing phyC displayed enhanced inhibition of hypocotyl elongation in Rc, but were unchanged in responsiveness to FRc relative to wild-type. These data indicate that phyC has photosensory specificity that is similar to that of phyB and thus distinct from that of phyA. phyC overexpressors with levels only 3 to 4 times the level of endogenous phyC exhibited enhanced primary leaf expansion in Wc. This is in contrast to phyA or phyB overexpressors which respectively have levels that are 50g-and 10g-fold that of overexpressed phyC but showed no enhancement of primary leaf expansion. Therefore, phyC may have some physiological roles that are different to those of phyA and phyB in the control of seedling responses to light signals.

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Progress in the Molecular Analysis of Phytochrome

Cited by 86 publications

References 81 publications

Isolation and Initial Characterization of Arabidopsis Mutants That Are Deficient in Phytochrome A

Isolation and Initial Characterization of Arabidopsis Mutants That Are Deficient in Phytochrome A

In vitro assembly of apophytochrome and apophytochrome deletion mutants expressed in yeast with phycocyanobilin.

Overexpressed phytochrome C has similar photosensory specificity to phytochrome B but a distinctive capacity to enhance primary leaf expansion

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