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Observation of early events in the photoactivation of Myxobacterial phytochrome using time-resolved serial femtosecond crystallography

Publiceringsår

2025

Upphovspersoner

Malla, Tek Narsingh; Aldama, Luis; Leon, Viridiana; Feliz, Denisse; Hu, Hao; Thomas, Isaiah; Cellini, Andrea; Wahlgren, Weixiao Y.; Nimmrich, Amke; Botha, Sabine; Sierra, Ray; Hunter, Mark S.; Poitevin, Frédéric; Lisova, Stella; Batyuk, Alexander; Gate, Gregory; Jernigan, Rebecca; Kupitz, Christopher J.; Maj, Piotr; Meszaros, Petra; Kurttila, Moona; Monrroy, Leonardo; Luo, Fangjia; Owada, Shigeki; Kang, Jungmin; Slavov, Chavdar; Maj, Michal; Gautier, Candice; Kashipathy, Maithri; Tolstikova, Alexandra; Mariani, Valerio; Barty, Anton; Moss, Frank; Schwander, Peter; Liu, Haiguang; Boutet, Sébastien; Fromme, Petra; Takala, Heikki; Ihalainen, Janne A.; Weierstall, Uwe; Westenhoff, Sebastian; Stojković, Emina A.; Schmidt, Marius
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Abstrakt

Myxobacteria are non-photosynthetic, soil-dwelling bacteria distinguished by a multicellular stage in their life cycle known as fruiting bodies that are stimulated by light. Myxobacterial phytochromes are candidates for the perception of red-light. The mechanism how light is perceived and converted to a physiological response is unknown. Here, time-resolved serial femtosecond crystallographic (TR-SFX) experiments were conducted on microcrystals of the photosensory core module of the Stigmatella aurantiaca bacteriophytochrome 2 (SaBphP2). Initial events of the Z to E isomerization reaction of the covalently bound, open-chain tetrapyrrole biliverdin (BV) chromophore were determined. At 3 ps after light activation, the BV ring-D assumes a configuration needed for the isomerization. At 100 ps, a mixture of BV in the Z or E configuration is observed in subunit A, while in the other subunit the chromophore remains in the Z configuration. In conjunction with prior results, these structures reveal the molecular mechanism of phytochrome activation in the photomorphogenesis of the myxobacteria and provide the molecular foundation for physiological responses to red light in other bacteria.
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Organisationer och upphovspersoner

Jyväskylä universitet

Takala Heikki Orcid -palvelun logo

Ihalainen Janne Orcid -palvelun logo

Kurttila Moona Orcid -palvelun logo

Publikationstyp

Publikationsform

Artikel

Moderpublikationens typ

Tidning

Artikelstyp

En originalartikel

Målgrupp

Vetenskaplig

Kollegialt utvärderad

Kollegialt utvärderad

UKM:s publikationstyp

A1 Originalartikel i en vetenskaplig tidskrift

Publikationskanalens uppgifter

Förläggare

Springer Nature

Volym

8

Artikelnummer

183

Publikationsforum

87037

Publikationsforumsnivå

1

Öppen tillgång

Öppen tillgänglighet i förläggarens tjänst

Ja

Öppen tillgång till publikationskanalen

Helt öppen publikationskanal

Parallellsparad

Ja

Övriga uppgifter

Vetenskapsområden

Biokemi, cell- och molekylärbiologi; Växtbiologi, mikrobiologi, virologi

Nyckelord

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Publiceringsland

Förenade kungariket

Förlagets internationalitet

Internationell

Språk

engelska

Internationell sampublikation

Ja

Sampublikation med ett företag

Nej

DOI

10.1038/s42004-025-01578-z

Publikationen ingår i undervisnings- och kulturministeriets datainsamling

Ja