Interaction between bacterial phytochromes Agp1 and Agp2 of Agrobacterium fabrum by fluorescence resonance energy transfer and docking studies DOI Creative Commons

Afaf El Kurdi,

Gero Kaeser, Patrick Scheerer

и другие.

FEBS Letters, Год журнала: 2025, Номер unknown

Опубликована: Янв. 26, 2025

Phytochromes are biliprotein photoreceptors found in bacteria, fungi, and plants. The soil bacterium Agrobacterium fabrum has two phytochromes, Agp1 Agp2, which work together to control DNA transfer plants bacterial conjugation. Both phytochromes interact as homodimeric proteins. For fluorescence resonance energy (FRET) measurements, various mutants wild-type Agp2 were labeled with specific fluorophores study their interaction. FRET efficiencies rose from position 122 545 of Agp1. photosensory chromophore module (PCM) did not show a signal, but the PCM did. Docking models suggest that histidine kinase perpendicular each, around 45 amino acids or involved.

Язык: Английский

Interaction between bacterial phytochromes Agp1 and Agp2 of Agrobacterium fabrum by fluorescence resonance energy transfer and docking studies DOI Creative Commons

Afaf El Kurdi,

Gero Kaeser, Patrick Scheerer

и другие.

FEBS Letters, Год журнала: 2025, Номер unknown

Опубликована: Янв. 26, 2025

Phytochromes are biliprotein photoreceptors found in bacteria, fungi, and plants. The soil bacterium Agrobacterium fabrum has two phytochromes, Agp1 Agp2, which work together to control DNA transfer plants bacterial conjugation. Both phytochromes interact as homodimeric proteins. For fluorescence resonance energy (FRET) measurements, various mutants wild-type Agp2 were labeled with specific fluorophores study their interaction. FRET efficiencies rose from position 122 545 of Agp1. photosensory chromophore module (PCM) did not show a signal, but the PCM did. Docking models suggest that histidine kinase perpendicular each, around 45 amino acids or involved.

Язык: Английский

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