Molecular basis for the selective and ABA-independent inhibition of PP2CA by PYL13.

TitleMolecular basis for the selective and ABA-independent inhibition of PP2CA by PYL13.
Publication TypeJournal Article
Year of Publication2013
AuthorsLi, W, Wang, L, Sheng, X, Yan, C, Zhou, R, Hang, J, Yin, P, Yan, N
JournalCell Res
Date Published2013 Dec
KeywordsAbscisic Acid, Amino Acid Sequence, Arabidopsis, Arabidopsis Proteins, Crystallography, X-Ray, Molecular Sequence Data, Phosphoprotein Phosphatases, Protein Binding, Protein Structure, Tertiary, Sequence Alignment, Sequence Homology, Amino Acid, Zinc Fingers

<p>PYR1/PYL/RCAR family proteins (PYLs) are well-characterized abscisic acid (ABA) receptors. Among the 14 PYL members in Arabidopsis thaliana, PYL13 is ABA irresponsive and its function has remained elusive. Here, we show that PYL13 selectively inhibits the phosphatase activity of PP2CA independent of ABA. The crystal structure of PYL13-PP2CA complex, which was determined at 2.4 Å resolution, elucidates the molecular basis for the specific recognition between PP2CA and PYL13. In addition to the canonical interactions between PYLs and PP2Cs, an extra interface is identified involving an element in the vicinity of a previously uncharacterized CCCH zinc-finger (ZF) motif in PP2CA. Sequence blast identified another 56 ZF-containing PP2Cs, all of which are from plants. The structure also reveals the molecular determinants for the ABA irresponsiveness of PYL13. Finally, biochemical analysis suggests that PYL13 may hetero-oligomerize with PYL10. These two PYLs antagonize each other in their respective ABA-independent inhibitions of PP2Cs. The biochemical and structural studies provide important insights into the function of PYL13 in the stress response of plant and set up a foundation for future biotechnological applications of PYL13.</p>

Alternate JournalCell Res
PubMed ID24165892
PubMed Central IDPMC3847573
Grant List / / Howard Hughes Medical Institute / United States