Light-induced structural changes in a monomeric bacteriophytochrome | Zendy

Heikki Takala | Zendy; Stephan Niebling | Zendy; Oskar Berntsson | Zendy; Alexander Björling | Zendy; Heli Lehtivuori | Zendy; Heikki Häkkänen | Zendy; Matthijs R. Panman | Zendy; Emil Gustavsson | Zendy; Maria Hoernke | Zendy; Gemma Newby | Zendy; Federico Zontone | Zendy; Michaël Wulff | Zendy; Andreas Menzel | Zendy; Janne A. Ihalainen | Zendy; Sebastian Westenhoff | Zendy

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Light-induced structural changes in a monomeric bacteriophytochrome

Author(s) -

Heikki Takala,

Stephan Niebling,

Oskar Berntsson,

Alexander Björling,

Heli Lehtivuori,

Heikki Häkkänen,

Matthijs R. Panman,

Emil Gustavsson,

Maria Hoernke,

Gemma Newby,

Federico Zontone,

Michaël Wulff,

Andreas Menzel,

Janne A. Ihalainen,

Sebastian Westenhoff

Publication year - 2016

Publication title -

structural dynamics

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.415

H-Index - 29

ISSN - 2329-7778

DOI - 10.1063/1.4961911

Subject(s) - phytochrome , deinococcus radiodurans , allosteric regulation , monomer , chromophore , phytochrome a , biophysics , chemistry , protein structure , crystallography , biochemistry , photochemistry , biology , dna , botany , arabidopsis , enzyme , red light , organic chemistry , gene , mutant , polymer

Phytochromes sense red light in plants and various microorganism. Light absorption causes structural changes within the protein, which alter its biochemical activity. Bacterial phytochromes are dimeric proteins, but the functional relevance of this arrangement remains unclear. Here, we use time-resolved X-ray scattering to reveal the solution structural change of a monomeric variant of the photosensory core module of the phytochrome from Deinococcus radiodurans. The data reveal two motions, a bend and a twist of the PHY domain with respect to the chromophore-binding domains. Infrared spectroscopy shows the refolding of the PHY tongue. We conclude that a monomer of the phytochrome photosensory core is sufficient to perform the light-induced structural changes. This implies that allosteric cooperation with the other monomer is not needed for structural activation. The dimeric arrangement may instead be intrinsic to the biochemical output domains of bacterial phytochromes.

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