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Identification of Interactions between Abscisic Acid and Ribulose-1,5-Bisphosphate Carboxylase/Oxygenase

Galka, Marek M ; Rajagopalan, Nandhakishore ; Buhrow, Leann M ; Nelson, Ken M ; Switala, Jacek ; Cutler, Adrian J ; Palmer, David R J ; Loewen, Peter C ; Abrams, Suzanne R ; Loewen, Michele C Berg, Ivan

PloS one, 2015-07, Vol.10 (7), p.e0133033-e0133033 [Periódico revisado por pares]

United States: Public Library of Science

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Título:
Identification of Interactions between Abscisic Acid and Ribulose-1,5-Bisphosphate Carboxylase/Oxygenase
Autor: Galka, Marek M ; Rajagopalan, Nandhakishore ; Buhrow, Leann M ; Nelson, Ken M ; Switala, Jacek ; Cutler, Adrian J ; Palmer, David R J ; Loewen, Peter C ; Abrams, Suzanne R ; Loewen, Michele C
Berg, Ivan
Assuntos: Abscisic acid ; Abscisic Acid - chemistry ; Abscisic Acid - metabolism ; Acids ; Affinity ; Amino Acid Sequence ; Analysis ; Arabidopsis - metabolism ; Arabidopsis thaliana ; Binding Sites ; Biochemistry ; Calorimetry ; Carbon ; Catalysis ; Catalytic activity ; Chemistry ; Councils ; Crystallography ; Docking ; Electron density ; Enzymes ; Molecular Sequence Data ; Monosaccharides ; Oxygenase ; Physiology ; Protein Binding ; Proteins ; Proteomics ; Ribulose-1,5-bisphosphate ; Ribulose-bisphosphate carboxylase ; Ribulose-Bisphosphate Carboxylase - chemistry ; Ribulose-Bisphosphate Carboxylase - metabolism ; Spinach ; Structural analysis ; Substrate inhibition ; Sugars ; Titration ; Titration calorimetry ; X-ray crystallography
É parte de: PloS one, 2015-07, Vol.10 (7), p.e0133033-e0133033
Notas: ObjectType-Article-1
SourceType-Scholarly Journals-1
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content type line 23
Competing Interests: The authors have declared that no competing interests exist.
Conceived and designed the experiments: MMG NR LB AJC DRJP SRA PCL MCL. Performed the experiments: MMG NR LB JS KMN PCL MCL. Analyzed the data: MMG NR LB JS KMN AJC DRJP PCL SRA MCL. Wrote the paper: MMG NR LB JS KMN AJC DRJP PCL SRA MCL.
Descrição: Abscisic acid ((+)-ABA) is a phytohormone involved in the modulation of developmental processes and stress responses in plants. A chemical proteomics approach using an ABA mimetic probe was combined with in vitro assays, isothermal titration calorimetry (ITC), x-ray crystallography and in silico modelling to identify putative (+)-ABA binding-proteins in crude extracts of Arabidopsis thaliana. Ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) was identified as a putative ABA-binding protein. Radiolabelled-binding assays yielded a Kd of 47 nM for (+)-ABA binding to spinach Rubisco, which was validated by ITC, and found to be similar to reported and experimentally derived values for the native ribulose-1,5-bisphosphate (RuBP) substrate. Functionally, (+)-ABA caused only weak inhibition of Rubisco catalytic activity (Ki of 2.1 mM), but more potent inhibition of Rubisco activation (Ki of ~ 130 μM). Comparative structural analysis of Rubisco in the presence of (+)-ABA with RuBP in the active site revealed only a putative low occupancy (+)-ABA binding site on the surface of the large subunit at a location distal from the active site. However, subtle distortions in electron density in the binding pocket and in silico docking support the possibility of a higher affinity (+)-ABA binding site in the RuBP binding pocket. Overall we conclude that (+)-ABA interacts with Rubisco. While the low occupancy (+)-ABA binding site and weak non-competitive inhibition of catalysis may not be relevant, the high affinity site may allow ABA to act as a negative effector of Rubisco activation.
Editor: United States: Public Library of Science
Idioma: Inglês

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Identification of Interactions between Abscisic Acid and Ribulose-1,5-Bisphosphate Carboxylase/Oxygenase

Galka, Marek M ; Rajagopalan, Nandhakishore ; Buhrow, Leann M ; Nelson, Ken M ; Switala, Jacek ; Cutler, Adrian J ; Palmer, David R J ; Loewen, Peter C ; Abrams, Suzanne R ; Loewen, Michele C Berg, Ivan

United States: Public Library of Science

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