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

El Kurdi, Afaf 1; Kaeser, Gero 1; Scheerer, Patrick; Hoffmann, David 2; Akkus, Ebru 2; Elstner, Marcus 2; Krauß, Norbert 1; Lamparter, Tilman 1
1 Joseph Gottlieb Kölreuter Institut für Pflanzenwissenschaften (JKIP), Karlsruher Institut für Technologie (KIT)
2 Institut für Physikalische Chemie (IPC), Karlsruher Institut für Technologie (KIT)

Abstract (englisch):

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


Verlagsausgabe §
DOI: 10.5445/IR/1000188949
Veröffentlicht am 18.12.2025
Cover der Publikation
Zugehörige Institution(en) am KIT Institut für Physikalische Chemie (IPC)
Joseph Gottlieb Kölreuter Institut für Pflanzenwissenschaften (JKIP)
Publikationstyp Zeitschriftenaufsatz
Publikationsmonat/-jahr 03.2025
Sprache Englisch
Identifikator ISSN: 0014-5793, 1873-3468
KITopen-ID: 1000188949
Erschienen in FEBS Letters
Verlag John Wiley and Sons
Band 599
Heft 6
Seiten 848–865
Vorab online veröffentlicht am 26.01.2025
Schlagwörter biliprotein, DNA transfer, histidine kinase, molecular docking, photoreceptor, protein interaction
Nachgewiesen in Scopus
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