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Photosystem II01:22

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The multi-protein complex photosystem II (PS II) harvests photons and transfers their energy through its bound pigments to its reaction center, and ultimately to photosystem I (PSI) through the electron transport chain. The pigments responsible for caputirng the light energy in photosystems include chlorophyll a, chlorophyll b, and carotenoids.
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Although structurally similar to photosystem II (PSII), photosystem I (PSI) is has a different electron supplier and electron acceptor.
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Anoxygenic photosynthesis is a phototrophic process that captures light energy to drive carbon fixation without producing molecular oxygen. Unlike oxygenic photosynthesis, which utilizes water as an electron donor and releases oxygen, anoxygenic phototrophs use alternative electron donors such as hydrogen sulfide (H₂S), elemental sulfur (S⁰), or thiosulfate (S₂O₃²⁻). This process is carried out by diverse groups of bacteria, including purple bacteria, green...
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Reaction centers are pigment-protein complexes that initiate energy conversion from photons to chemical entities. Therefore, photochemical reaction center is a more appropriate term that describes these complexes. The Nobel laureates Robert Emerson and William Arnold provided the first experimental evidence of photochemical reaction centers by demonstrating the participation of nearly 2,500 chlorophyll molecules for the release of just one molecule of oxygen. Despite thousands of photosynthetic...
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The addition or removal of phosphate groups from proteins is the most common chemical modification that regulates cellular processes. These modifications can affect the structure, activity, stability, and localization of proteins within cells as well as their interactions with other proteins.
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Membrane lipids such as phosphatidylinositol (PI) are precursors for several membrane-bound and soluble second messengers. Specific kinases phosphorylate PI and produce phosphorylated inositol phospholipids. One such inositol phospholipids are the  phosphatidylinositol-4,5 bisphosphate [PI(4,5)P2], present in the inner half of the lipid bilayer. Upon ligand binding, GPCR stimulates Gq proteins to turn on phospholipase Cꞵ. Activated phospholipase Cꞵ cleaves PI(4,5)P2 and...
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Mode of autophosphorylation in bacteriophytochromes RpBphP2 and RpBphP3.

Indika Kumarapperuma1, Irin P Tom1, Sepalika Bandara1

  • 1Department of Chemistry, University of Illinois Chicago, Chicago, IL, USA.

Photochemical & Photobiological Sciences : Official Journal of the European Photochemistry Association and the European Society for Photobiology
|February 9, 2023
PubMed
Summary

Phytochromes are light sensors. This study reveals that bacteriophytochromes, a type of phytochrome, use light-dependent trans-phosphorylation for kinase activation, clarifying their signaling mechanism.

Keywords:
AutophosphorylationBacteriophytochromeCrystal structureKinase activationPhotoreceptorSensory histidine kinase

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Microbiology

Background:

  • Phytochromes are crucial red-light photoreceptors in various organisms.
  • Bacteriophytochromes function as photosensory histidine kinases in two-component signaling pathways.
  • The precise mechanism of kinase activation and autophosphorylation directionality in bacteriophytochromes remains unclear.

Purpose of the Study:

  • To investigate the molecular mechanism of kinase activation in bacteriophytochromes.
  • To determine the directionality of autophosphorylation in bacteriophytochromes.
  • To elucidate the role of light in regulating bacteriophytochrome kinase activity.

Main Methods:

  • Histidine kinase assays were performed on full-length bacteriophytochromes (RpBphP2 and RpBphP3) and loss-of-function mutants.
  • Kinase activities were analyzed under varying light conditions.
  • Crystal structure of the histidine kinase domains of RpBphP2 was determined at 3.19 Å resolution.

Main Results:

  • RpBphP2 and RpBphP3 exhibit light-dependent trans-phosphorylation between protomers.
  • This trans-phosphorylation occurs in both homodimeric and heterodimeric forms.
  • A structural model for trans-autophosphorylation in bacteriophytochromes was proposed based on crystal structure and homology modeling.

Conclusions:

  • Bacteriophytochromes utilize light-dependent trans-phosphorylation for kinase activation.
  • This finding clarifies a key step in the signal transduction pathway regulated by bacteriophytochromes.
  • The study provides a structural basis for understanding bacteriophytochrome function.