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Concepts in Photobiology pp 755–795Cite as

Phytochromes: molecular structure, photoreceptor process and physiological function

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Summary

Phytochrome (P)—a unique photochromic pigment—mediates a great variety of photoregulation reactions in plants thus determining the strategy of their optimum light development, i.e. photomorphogenesis. The pigment molecule is a dimer whose identical monomers consist of a linear tetrapyrrole covalently bound to a ca 125 kDa water soluble protein comprising ca 1200 amino acid residues. The monomer is structurally divided into an N-terminal chromophore bearing domain responsible for light perception and a C-terminal domain responsible for dimerization and light stimulus transduction. The spectroscopical and photochemical properties of the pigment are determined by the specific chromophore-apoprotein interaction. Its photoperception function is based on the photoreversible phototransformation of the initial red-light—absorbing form (Pr) into a physiologically active far-red-light—absorbing form (Pfr). The Pr → Pfr conversion includes an energy storing photoreaction, which is cis-trans photoisomerization of the chromophore proceeding within several tens ps with participation of the singlet excited state, and a following branched dark stepwise protein relaxation leading to its conformationally restructured form. The functional activity of the Pfr form is connected with the rearrangement of a number of amino acid residues in the C-terminal. The transduction of the signal from the Pfr form includes activation of a putative primary receptor (G-proteins) and changes of the concentration of Ca2+ and cyclic guanosine 5′-phosphate (cGMP) leading eventually to the modulation of the rate of gene expression. Action of P as a light-regulated enzyme is also considered as a possible mechanism of signal transduction. The complex behaviour of plants under different light conditions and the multiple functions of P are believed to be connected, at least in part, with heterogeneity of the pigment in the cell and first of all with the existence of a small family of Ps (five or more depending on plant species) which are encoded by different genes but possess the same chromophore. The main ones, phytochromes A and B (phyA and phyB), perform different functions or complement each other in some responses as shown by the investigations of P mutants. PhyA itself is found to be heterogeneous: it consists of two spectroscopically, photochemically and functionally distinct species: the major soluble and labile phyA’ and a minor presumably membrane-associated and relatively stable phyA”. Dimeric structure of the photoreceptor is also suggested to be a potential source of the multiple action of the pigment. And finally, it is believed that photoreactions of the intermediates of the P cycle can modify the P functions. Thus, investigation of the structure-function relationship in the P molecule acquires now a new dimension for understanding of the physiological polyfunctionality of the pigment.

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  1. Biology Faculty, M.V. Lomonosov, Moscow State University, 119899, Moscow, Russia

    Vitally A. Sineshchekov

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  1. School of Life Sciences, Jawaharlal Nehru University, New Delhi, India

    G. S. Singhal

  2. Technische Universität, Berlin, Germany

    G. Renger  & K.-D. Irrgang  & 

  3. International Centre for Genetic Engineering and Biotechnology, New Delhi, India

    S. K. Sopory

  4. University of Illinois at Urbana Champaign, Urbana, IL, USA

    Govindjee

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Sineshchekov, V.A. (1999). Phytochromes: molecular structure, photoreceptor process and physiological function. In: Singhal, G.S., Renger, G., Sopory, S.K., Irrgang, KD., Govindjee (eds) Concepts in Photobiology. Springer, Dordrecht. https://doi.org/10.1007/978-94-011-4832-0_25

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