Molecular Properties of Phytochrome

Pratt, Lee H.

doi:10.1111/j.1751-1097.1978.tb07569.x

Cited by 150 publications

(87 citation statements)

References 146 publications

(140 reference statements)

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“…4, D-F). Consequently, these molecules are less stable in their physiological Pfr form, which is consistent with the previous observation that the N terminus is very important for the stability of the Pfr form of phytochrome (40). We conclude that, among other factors, the very N-terminal part of the monocotyledonous phyA is necessary, but not sufficient, for the prevention of dark reversion.…”

Section: Table I Expression Of Phytochrome Constructs In Yeastsupporting

confidence: 79%

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In Vivo Characterization of Chimeric Phytochromes in Yeast

Eichenberg

Kunkel

Kretsch

et al. 1999

Journal of Biological Chemistry

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Phytochromes are plant photoreceptors that play a major role in photomorphogenesis. Two members of the phytochrome family have been characterized in some detail. Phytochrome A, which controls very low fluence and high irradiance responses, is rapidly degraded in the light, forms sequestered areas of phytochrome (SAPs), and does not exhibit dark reversion in monocotyledonous seedlings. Phytochrome B mediates red/ far-red reversible responses, is stable in the light, and does not form SAPs. We report on the behavior in yeast of the phytochrome apoproteins of rice PHYA, tobacco PHYB, and chimeric PHYAB and PHYBA and on the behavior of the respective holoprotein adducts after assembly with phycocyanobilin chromophore (PHY*). SAP-like formation in yeast was not observed for PHYB, but was detectable for PHYA, PHYAB, and PHYBA. Rice PHYA* did not undergo dark reversion in yeast. Surprisingly, all other tested phytochrome constructs did exhibit dark reversion, including chimeric phytochromes with a short N-terminal part of tobacco PHYB or parsley PHYA fused to rice PHYA. Furthermore, the proportion of phytochrome undergoing dark reversion and the rate of reversion were increased for both the N terminusswapped constructs and PHYBA*. These results are discussed with respect to structure/function analysis of phytochromes A and B.

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Section: Table I Expression Of Phytochrome Constructs In Yeastsupporting

confidence: 79%

“…In vitro dark reversion of extracts of potato PHYA* and PHYB* expressed in yeast was shown by Ruddat et al (39). In vitro dark reversion of oat phyA is detectable only for the so-called large phytochrome, which lacks the 4 -6-kDa N-terminal fragment (40).…”

Section: Table I Expression Of Phytochrome Constructs In Yeastmentioning

confidence: 99%

In Vivo Characterization of Chimeric Phytochromes in Yeast

Eichenberg

Kunkel

Kretsch

et al. 1999

Journal of Biological Chemistry

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“…Under these conditions, the degradation of the tetrapyrrole is accompanied by oxidation of the thio ether to sulfone Η (U) (14), which eliminates -S0 2 -C 2 H 5 to give (6) {5 * ] in the presence of aqueous ammonia. This reaction sequence not only demonstrates the protein-bond of ring A, it is also ste-reoselective 145 58 591 and leads, with the well-known 4R,Econfiguration of the imide (6a) [5(i \ to the 2Ä,3Ä;3jR-configuration of (la), (lb), (2) and (3).…”

Section: Pcpementioning

confidence: 99%

Biliproteins

Scheer¹

1981

Angew. Chem. Int. Ed. Engl.

151

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“…In either case, the question of whether the final binding step follows spontaneously in the cell or is induced artifactually by the preparative procedure remains to be determined (8,10).…”

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confidence: 99%

“…8 for comprehensive discussion). This in vivo phase of the phenomenon is initiated upon Pfr formation and requires the continued presence of this form of the pigment for a finite period in the cell to allow the process to run to completion.…”

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confidence: 99%

Irradiation-enhanced Phytochrome Pelletability

Quail¹,

Briggs²

1978

Plant Physiol.

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Short, high intensity pulses of red and far red light are used to study, at room temperature, the kinetics of the In vivo dark reaction responsible for irradiation-enhanced phytochrome pelletability. The t1/2 for this reaction is 2 seconds at 25 C in both Avena shoots and Zea mays coleoptiles. This is the most rapid phytochrome-far red-absorbing form (Pfr)-mediated cellular response thus far reported. Anoxia, KCN, NaN3 and carbonyl cyanide p-trifluoromethoxyphenylhydrazone reduce the rate (but not the final extent) of the reaction by more than an order of magnitude. The rate of the reaction under these conditions is strongly correlated with the inhibitor-induced reductions in cellular ATP levels. Likewise, recovery in ATP levels upon withdrawal of the inhibitors is accompanied by a parallel recovery in the rate of the reaction. Cytochalasin B blocks cytoplasmic streaming without diminishing the pelletability response. Colchicine is likewise without effect. These data suggest a requirement for phosphorylative energy in one or more of the Pfr-dependent intracellular events leading to enhanced phytochrome pelletability. The possibility that this event might represent an ATP-dependent modification of the pigment protein itself in the Pfr form is discussed.

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Molecular Properties of Phytochrome

Cited by 150 publications

References 146 publications

In Vivo Characterization of Chimeric Phytochromes in Yeast

In Vivo Characterization of Chimeric Phytochromes in Yeast

Biliproteins

Irradiation-enhanced Phytochrome Pelletability

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