Long-range signaling mechanism of a bacteriophytochrome at the atomic level (Comunicación Oral)

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

Mendoza

Congreso; LVIII Reunión Anual de la SAIB; 2022

Sociedad Argentina de Investigaciones en Bioquímica y Biología Molecular (SAIB)

Phytochromes are photo‐sensing proteins distributed among plants, fungi and prokaryotes, including pathogens, which reversibly photoconverted, between a red‐absorbing (Pr) and a far‐red‐absorbing (Pfr) state. Despite the vast structural information currently reported, their dynamic protein structures are an extremely challenging matter in structural photobiology where several key questions still remain to be answered. Undoubtedly, one of the most relevant interrogates is how the long‐range structural changes are propagated from the light‐sensing module (Photosensory Module) to the effector module (Output Module) during the Pr‐Pfr photoconversion. This question remains elusive essentially due to two causes: i) Overwhelmingly, most reported phytochrome structures are truncated versions, without a complete Output Module. ii) No full‐length phytochrome structures have been solved at the atomic level in both pure Pr and Pfr photostates. Our group has recently reported a complete structural characterization at the atomic level of the bacteriophytochrome from the phytopathogenic Xanthomonas campestris (including two full‐length versions) in the Pr and Pfr states. In this talk, the light‐driven conformational changes during the reversible photoswitching in a full‐length phytochrome will be exposed.