PLAT domain protein 1 (PLAT1/PLAFP) binds to the Arabidopsis thaliana plasma membrane and inserts a lipid.

Autor: Kulke M; Plant Research Laboratory, Michigan State University, East Lansing 48824, MI, USA., Kurtz E; Department Of Biochemistry and Molecular Biology, Michigan State University, East Lansing 48824, MI, USA., Boren DM; Plant Research Laboratory, Michigan State University, East Lansing 48824, MI, USA; Department Of Biochemistry and Molecular Biology, Michigan State University, East Lansing 48824, MI, USA., Olson DM; Department Of Biochemistry and Molecular Biology, Michigan State University, East Lansing 48824, MI, USA., Koenig AM; Department Of Biochemistry and Molecular Biology, Michigan State University, East Lansing 48824, MI, USA., Hoffmann-Benning S; Department Of Biochemistry and Molecular Biology, Michigan State University, East Lansing 48824, MI, USA. Electronic address: hoffma16@msu.edu., Vermaas JV; Plant Research Laboratory, Michigan State University, East Lansing 48824, MI, USA; Department Of Biochemistry and Molecular Biology, Michigan State University, East Lansing 48824, MI, USA. Electronic address: vermaasj@msu.edu.
Jazyk: angličtina
Zdroj: Plant science : an international journal of experimental plant biology [Plant Sci] 2024 Jan; Vol. 338, pp. 111900. Date of Electronic Publication: 2023 Oct 19.
DOI: 10.1016/j.plantsci.2023.111900
Abstrakt: Robust agricultural yields depend on the plant's ability to fix carbon amid variable environmental conditions. Over seasonal and diurnal cycles, the plant must constantly adjust its metabolism according to available resources or external stressors. The metabolic changes that a plant undergoes in response to stress are well understood, but the long-distance signaling mechanisms that facilitate communication throughout the plant are less studied. The phloem is considered the predominant conduit for the bidirectional transport of these signals in the form of metabolites, nucleic acids, proteins, and lipids. Lipid trafficking through the phloem in particular attracted our attention due to its reliance on soluble lipid-binding proteins (LBP) that generate and solubilize otherwise membrane-associated lipids. The Phloem Lipid-Associated Family Protein (PLAFP) from Arabidopsis thaliana is generated in response to abiotic stress as is its lipid-ligand phosphatidic acid (PA). PLAFP is proposed to transport PA through the phloem in response to drought stress. To understand the interactions between PLAFP and PA, nearly 100 independent systems comprised of the protein and one PA, or a plasma membrane containing varying amounts of PA, were simulated using atomistic classical molecular dynamics methods. In these simulations, PLAFP is found to bind to plant plasma membrane models independent of the PA concentration. When bound to the membrane, PLAFP adopts a binding pose where W41 and R82 penetrate the membrane surface and anchor PLAFP. This triggers a separation of the two loop regions containing W41 and R82. Subsequent simulations indicate that PA insert into the β-sandwich of PLAFP, driven by interactions with multiple amino acids besides the W41 and R82 identified during the insertion process. Fine-tuning the protein-membrane and protein-PA interface by mutating a selection of these amino acids may facilitate engineering plant signaling processes by modulating the binding response.
Competing Interests: Declaration of Competing Interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.
(Copyright © 2023 Elsevier B.V. All rights reserved.)
Databáze: MEDLINE
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