Light-induced structural changes during the signaling mechanism of a full-length bacteriophytochrome

ANTELO, GIULIANO T.; KLINKE, SEBASTIÁN; BATTOCCHIO, GIOVANNI; CHAVAS, LEONARDO; RINALDI, JIMENA; FOSCALDI, SABRINA; SIRIGU, SERENA; SÁNCHEZ-LAMAS, MAXIMILIANO; VOJNOV, ADRIAN; MROGINSKI, MARÍA ANDREA; OTERO, LISANDRO H.; ROSANO, GERMAN L.; DEFELIPE, LUCAS A.; CONFORTE, VALERIA; GOLDBAUM, FERNANDO A.; BONOMI, HERNAN R.

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Conferencia; Bringing Molecular Structure to Life: 50 Years of the PDB - EMBL; 2021

EMBL

Light sensing allows organisms to adapt to constantly changing environmental factors. Phytochromes constitute a major superfamily of light-sensing proteins that are reversibly photoconverted between a red-absorbing (Pr) and a far-red-absorbing (Pfr) state. Bacteriophytochromes (BphPs) are found among photosynthetic and non-photosynthetic bacteria, including pathogens. To date, several BphPs have been biophysically characterized.However, it is still not fully understood how structural changes are propagated from the photosensory module to the output module during the signal transduction event. Herein, we present crystallographic structures from the plant pathogen Xanthomonas campestris virulence regulator bacteriophytochrome, including two full-length proteins, in the Pr and Pfr states. The structural findings, combined with mutational, biochemical and computational studies, allow us to describe the signaling mechanism of a full-length bacterialphytochrome at the atomic level, from the isomerization of the chromophore and the β-sheet/α-helixtongue transition to the remodeling of the quaternary assembly of the protein. This work contributes to understand the light-induced structural changes propagated from the photosensor to the output modules in phytochrome signaling.p { margin-bottom: 0.25cm; line-height: 115% }a:link { so-language: zxx }