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Article: Thermodynamic insights into an interaction between ACYL-CoA–BINDING PROTEIN2 and LYSOPHOSPHOLIPASE2 in Arabidopsis
Title | Thermodynamic insights into an interaction between ACYL-CoA–BINDING PROTEIN2 and LYSOPHOSPHOLIPASE2 in Arabidopsis |
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Authors | |
Issue Date | 2019 |
Publisher | American Society for Biochemistry and Molecular Biology, Inc. The Journal's web site is located at http://www.jbc.org/ |
Citation | Journal of Biological Chemistry, 2019, v. 294 n. 16, p. 6214-6226 How to Cite? |
Abstract | Lysophospholipids (LPLs) are important lipid-signaling molecules in plants, of which lysophosphatidylcholine (lysoPC) is one of the most well-characterized LPLs, having important roles in plant stress responses. It is broken down by lysophospholipases, but the molecular mechanism involved in lysoPC degradation is unclear. Recombinant Arabidopsis thaliana ACYL-COA-BINDING PROTEIN2 (AtACBP2) has been reported to bind lysoPC via its acyl-CoA-binding domain and also LYSOPHOSPHOLIPASE 2 (AtLYSOPL2) via its ankyrin repeats in vitro To investigate the interactions of AtACBP2 with AtLYSOPL2 and lysoPC in more detail, we conducted isothermal titration calorimetry (ITC) with AtACBP270-354, an AtACBP2 derivative consisting of amino acids 70-354, containing both the acyl-CoA-binding domain and ankyrin repeats. We observed that the interactions of AtACBP270-354 with AtLYSOPL2 and with lysoPC were both endothermic, favored by solvation entropy and opposed by enthalpy, with dissociation constants in the micromolar range. Of note, three AtLYSOPL2 catalytic triad mutant proteins (S147A, D268A, and H298A) bound lysoPC only weakly, with an exothermic burst and dissociation constants in the millimolar range. Furthermore, the binding affinity of lysoPC-premixed AtACBP270-354 to AtLYSOPL2 was 10-fold higher than that of AtACBP270-354 alone to AtLYSOPL2. We conclude that AtACBP2 may play a role in facilitating a direct interaction between AtLYSOPL2 and lysoPC. Our results suggest that AtACBP270-354 probably binds to lysoPC through a hydrophobic interface that enhances a hydrotropic interaction of AtACBP270-354 with AtLYSOPL2 and thereby facilitates AtLYSOPL2's lysophospholipase function. |
Persistent Identifier | http://hdl.handle.net/10722/269416 |
ISSN | 2020 Impact Factor: 5.157 2023 SCImago Journal Rankings: 1.766 |
PubMed Central ID | |
ISI Accession Number ID |
DC Field | Value | Language |
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dc.contributor.author | Miao, R | - |
dc.contributor.author | Lung, SC | - |
dc.contributor.author | Li, X | - |
dc.contributor.author | Li, XD | - |
dc.contributor.author | Chye, ML | - |
dc.date.accessioned | 2019-04-24T08:07:16Z | - |
dc.date.available | 2019-04-24T08:07:16Z | - |
dc.date.issued | 2019 | - |
dc.identifier.citation | Journal of Biological Chemistry, 2019, v. 294 n. 16, p. 6214-6226 | - |
dc.identifier.issn | 0021-9258 | - |
dc.identifier.uri | http://hdl.handle.net/10722/269416 | - |
dc.description.abstract | Lysophospholipids (LPLs) are important lipid-signaling molecules in plants, of which lysophosphatidylcholine (lysoPC) is one of the most well-characterized LPLs, having important roles in plant stress responses. It is broken down by lysophospholipases, but the molecular mechanism involved in lysoPC degradation is unclear. Recombinant Arabidopsis thaliana ACYL-COA-BINDING PROTEIN2 (AtACBP2) has been reported to bind lysoPC via its acyl-CoA-binding domain and also LYSOPHOSPHOLIPASE 2 (AtLYSOPL2) via its ankyrin repeats in vitro To investigate the interactions of AtACBP2 with AtLYSOPL2 and lysoPC in more detail, we conducted isothermal titration calorimetry (ITC) with AtACBP270-354, an AtACBP2 derivative consisting of amino acids 70-354, containing both the acyl-CoA-binding domain and ankyrin repeats. We observed that the interactions of AtACBP270-354 with AtLYSOPL2 and with lysoPC were both endothermic, favored by solvation entropy and opposed by enthalpy, with dissociation constants in the micromolar range. Of note, three AtLYSOPL2 catalytic triad mutant proteins (S147A, D268A, and H298A) bound lysoPC only weakly, with an exothermic burst and dissociation constants in the millimolar range. Furthermore, the binding affinity of lysoPC-premixed AtACBP270-354 to AtLYSOPL2 was 10-fold higher than that of AtACBP270-354 alone to AtLYSOPL2. We conclude that AtACBP2 may play a role in facilitating a direct interaction between AtLYSOPL2 and lysoPC. Our results suggest that AtACBP270-354 probably binds to lysoPC through a hydrophobic interface that enhances a hydrotropic interaction of AtACBP270-354 with AtLYSOPL2 and thereby facilitates AtLYSOPL2's lysophospholipase function. | - |
dc.language | eng | - |
dc.publisher | American Society for Biochemistry and Molecular Biology, Inc. The Journal's web site is located at http://www.jbc.org/ | - |
dc.relation.ispartof | Journal of Biological Chemistry | - |
dc.rights | This research was originally published in the Journal of Biological Chemistry. Rui Miao, Shiu-Cheung Lung, Xin Li, Xiang David Li and Mee-Len Chye. Thermodynamic Insights Into An Interaction Between Acyl-coa-binding Protein2 And Lysophospholipase2 In Arabidopsis. Journal of Biological Chemistry. 2019. 294:6214-6226. © the Author(s). | - |
dc.rights | This work is licensed under a Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License. | - |
dc.title | Thermodynamic insights into an interaction between ACYL-CoA–BINDING PROTEIN2 and LYSOPHOSPHOLIPASE2 in Arabidopsis | - |
dc.type | Article | - |
dc.identifier.email | Lung, SC: sclung@hku.hk | - |
dc.identifier.email | Li, X: lx418@hku.hk | - |
dc.identifier.email | Li, XD: xiangli@hku.hk | - |
dc.identifier.email | Chye, ML: mlchye@hku.hk | - |
dc.identifier.authority | Li, XD=rp01562 | - |
dc.identifier.authority | Chye, ML=rp00687 | - |
dc.description.nature | published_or_final_version | - |
dc.identifier.doi | 10.1074/jbc.RA118.006876 | - |
dc.identifier.pmid | 30782848 | - |
dc.identifier.pmcid | PMC6484133 | - |
dc.identifier.scopus | eid_2-s2.0-85064872946 | - |
dc.identifier.hkuros | 297530 | - |
dc.identifier.hkuros | 297933 | - |
dc.identifier.volume | 294 | - |
dc.identifier.issue | 16 | - |
dc.identifier.spage | 6214 | - |
dc.identifier.epage | 6226 | - |
dc.identifier.isi | WOS:000468402000002 | - |
dc.publisher.place | United States | - |
dc.identifier.issnl | 0021-9258 | - |