Chromopeptides from phytochrome. The structure and linkage of the PR form of the phytochrome chromophore

Lagarias, J. Clark; Rapoport, Henry

doi:10.1021/ja00534a042

Cited by 296 publications

(276 citation statements)

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“…Clearly, the complex bilin-binding site of phytochromes stabilizes these P fr photo states by an unresolved mechanism, e.g. by electrostatic interaction, steric control of bilin conformation, or even formation of enol-like tautomers (44). Our structural and mutagenesis data on SynCph2 indicate that the conserved PRXSF, W(G/A)G, and WXE motifs of the tongue region are crucial for P fr formation.…”

Section: Table 2 Ring Tilts Of Pcb From X-ray Crystallography and Qm/mentioning

confidence: 87%

Structure of the Cyanobacterial Phytochrome 2 Photosensor Implies a Tryptophan Switch for Phytochrome Signaling

Anders

Daminelli-Widany

Mroginski

et al. 2013

Journal of Biological Chemistry

168

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Background: Phytochromes are red/far-red photoreceptors using a bilin chromophore. Results: Compared with Cph1, the Cph2 bilin-binding site differs around the propionates, but utilizes an otherwise conserved tongue for sealing the chromophore from solvent. Conclusion:The tongue signals via a tryptophan switch within the tongue-GAF domain interface. Significance: The first structure of a Cph2-type phytochrome indicates a common mechanism for photoswitching in all canonical phytochromes.

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Section: Table 2 Ring Tilts Of Pcb From X-ray Crystallography and Qm/mentioning

confidence: 87%

Structure of the Cyanobacterial Phytochrome 2 Photosensor Implies a Tryptophan Switch for Phytochrome Signaling

Anders

Daminelli-Widany

Mroginski

et al. 2013

Journal of Biological Chemistry

168

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“…Post-transcriptional steps that affect mRNA abundances include intron splicing, 5' and 3' transcript processing, as well as preferential mRNA stabilization (Gruissem, 1989). Translational regulation was also implicated as being involved in the control of plastid protein formation Laing et al, 1988;Danon and Mayfield, 1991;Eichacker et al, 1992).…”

Section: Morphological Cellular and Molecular Events During The Ligmentioning

confidence: 99%

“…Phytochromobilin is covalently bound to the phytochrome apoprotein (Lagarias and Rapoport, 1980), and this holocomplex is known to act as a photoreceptor that controls various developmental processes (Furuya, 1993 ;Kendrick and Kronenberg, 1994). In plants and many bacteria, all of the different tetrapyrroles seem to originate from a common biosynthetic pathway (Beale and Weinstein, 1990).…”

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confidence: 99%

The Regulation of Enzymes Involved in Chlorophyll Biosynthesis

Reinbothe

1996

European Journal of Biochemistry

125

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All living organisms contain tetrapyrroles. In plants, chlorophyll (chlorophyll a plus chlorophyll b) is the most abundant and probably most important tetrapyrrole. It is involved in light absorption and energy transduction during photosynthesis. Chlorophyll is synthesized from the intact carbon skeleton of glutamate via the C, pathway. This pathway takes place in the chloroplast. It is the aim of this review to summarize the current knowledge on the biochemistry and molecular biology of the C,-pathway enzymes, their regulated expression in response to light, and the impact of chlorophyll biosynthesis on chloroplast development. Particular emphasis will be placed on the key regulatory steps of chlorophyll biosynthesis in higher plants, such as 5-aminolevulinic acid formation, the production of Mg*+-protoporphyrin IX, and light-dependent protochlorophyllide reduction.

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“…Analogous results have been obtained when proteolytic digestion is used in stead for the uncoupling of the chromophore 1551 . The A-dihydrobilindione structure of the chromophores (la) and (lb) and the thioether-bond have recently been proved, too, by NMR spectroscopy of the respective bilipeptides* 38 ' 651 . This method also afforded independent proof of the presence of the 18-vinyl group in (lb) m .…”

Section: Cooch3mentioning

confidence: 99%