Chromophores in Photomorphogenesis

Rüdiger, W.; Scheer, Hugo

doi:10.1007/978-3-642-68918-5_7

Cited by 16 publications

(10 citation statements)

References 148 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The lightexcited chromophore isomerizes to the Pfr form (45), eventually influencing the structure and surface properties of the phytochrome protein (46). Hence, characterization of the molecular interaction between the chromophore and the apoprotein is crucial for understanding the functional mechanism(s) of phytochromes.…”

Section: Discussionmentioning

confidence: 99%

In vitro assembly of phytochrome B apoprotein with synthetic analogs of the phytochrome chromophore

Hanzawa

Inomata

Kinoshita

et al. 2001

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

View full text Add to dashboard Cite

Phytochrome B (PhyB), one of the major photosensory chromoproteins in plants, mediates a variety of light-responsive developmental processes in a photoreversible manner. To analyze the structural requirements of the chromophore for the spectral properties of PhyB, we have designed and chemically synthesized 20 analogs of the linear tetrapyrrole (bilin) chromophore and reconstituted them with PhyB apoprotein (PHYB). The A-ring acts mainly as the anchor for ligation to PHYB, because the modification of the side chains at the C2 and C3 positions did not significantly influence the formation or difference spectra of adducts. In contrast, the side chains of the B-and C-rings are crucial to position the chromophore properly in the chromophore pocket of PHYB and for photoreversible spectral changes. The side-chain structure of the D-ring is required for the photoreversible spectral change of the adducts. When methyl and ethyl groups at the C17 and C18 positions are replaced with an n-propyl, n-pentyl, or n-octyl group, respectively, the photoreversible spectral change of the adducts depends on the length of the side chains. From these studies, we conclude that each pyrrole ring of the linear tetrapyrrole chromophore plays a different role in chromophore assembly and the photochromic properties of PhyB.

show abstract

Section: Discussionmentioning

confidence: 99%

In vitro assembly of phytochrome B apoprotein with synthetic analogs of the phytochrome chromophore

Hanzawa

Inomata

Kinoshita

et al. 2001

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

View full text Add to dashboard Cite

show abstract

“…This species is a dimer of 124-kD subunits (Jones and Quail 1986), each of which contains a covalently attached linear tetrapyrrole chromophore (Rudiger and Scheer 1983). The complete amino acid sequences of the abundant, etiolated-tissue phytochrome from oat , zucchini (Sharrock et al 1986), pea (Sato 1988), rice (Kay et al 1989a), and com (Christensen and Quail 1989), have been derived from the corresponding nucleic acid sequences.…”

mentioning

confidence: 99%

Novel phytochrome sequences in Arabidopsis thaliana: structure, evolution, and differential expression of a plant regulatory photoreceptor family.

Sharrock¹,

Quail²

1989

Genes Dev.

795

678

View full text Add to dashboard Cite

Phytochrome is a plant regulatory photoreceptor that mediates red light effects on a wide variety of physiological and molecular responses. DNA blot analysis indicates that the Arabidopsis thaliana genome contains four to five phytochrome-related gene sequences. We have isolated and sequenced cDNA clones corresponding to three of these genes and have deduced the amino acid sequence of the full-length polypeptide encoded in each case. One of these proteins ipbyA) shows 65-80% amino acid sequence identity with the major, etiolated-tissue phytochrome apoproteins described previously in other plant species. The other two polypeptides {pbyB and pbyC) are unique in that they have low sequence identity (-50%) with each other, with pbyA, and with all previously described phytochromes. The pbyA, pbyB, and pbyC proteins are of similar molecular mass, have related hydropathic profiles, and contain a conserved chromophore attachment region. However, the sequence comparison data indicate that the three pby genes diverged early in plant evolution, well before the divergence of the two major groups of angiosperms, the monocots and dicots. The steady-state level of the pbyA transcript is high in dark-grown A. tbaliana seedlings and is down-regulated by light. In contrast, the pbyB and pbyC transcripts are present at lower levels and are not strongly light-regulated. These findings indicate that the red/far red light-responsive phytochrome photoreceptor system in A. tbaliana, and perhaps in all higher plants, consists of a family of chromoproteins that are heterogeneous in structure and regulation.

show abstract

“…Phytochrome is a protein with a molecular mass of 120 to 127 kilodaltons, depending on plant species (66), covalently linked with a linear tetrapyrrole chromophore (51). Interactions between the polypeptide and chromophore endow the photoreceptor with unique spectral properties that allow it to exist in two photointerconvertible forms: Pr, which absorbs maximally in the red (R) (Xmax = 666 nm) region of the spectrum, and Pfr, which absorbs maximally in the far-red (FR) (Xmax = 730 nm) region.…”

mentioning

confidence: 99%

Rapid transcriptional regulation by phytochrome of the genes for phytochrome and chlorophyll a/b-binding protein in Avena sativa.

Lissemore¹,

Quail²

1988

Mol. Cell. Biol.

119

113

View full text Add to dashboard Cite

show abstract

Chromophores in Photomorphogenesis

Cited by 16 publications

References 148 publications

In vitro assembly of phytochrome B apoprotein with synthetic analogs of the phytochrome chromophore

In vitro assembly of phytochrome B apoprotein with synthetic analogs of the phytochrome chromophore

Novel phytochrome sequences in Arabidopsis thaliana: structure, evolution, and differential expression of a plant regulatory photoreceptor family.

Rapid transcriptional regulation by phytochrome of the genes for phytochrome and chlorophyll a/b-binding protein in Avena sativa.

Contact Info

Product

Resources

About