Potent ABA‐independent activation of engineered PYL3
| العنوان: | Potent ABA‐independent activation of engineered PYL3 |
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| المؤلفون: | Xiangtao Wu, Xingliang Zhang, Weihong Lu, Yutao Wang, Chong Feng, Xiaoli Zhang |
| المصدر: | FEBS Open Bio FEBS Open Bio, Vol 11, Iss 5, Pp 1428-1439 (2021) |
| بيانات النشر: | John Wiley and Sons Inc., 2021. |
| سنة النشر: | 2021 |
| مصطلحات موضوعية: | 0301 basic medicine, HAB1, QH301-705.5, Mutant, Phosphatase, Arabidopsis, Mutagenesis (molecular biology technique), Receptors, Cell Surface, Genetically modified crops, constitutive inhibition, Naphthalenes, General Biochemistry, Genetics and Molecular Biology, PYL3, 03 medical and health sciences, chemistry.chemical_compound, 0302 clinical medicine, Stress, Physiological, Phosphoprotein Phosphatases, Biology (General), Receptor, Abscisic acid, Research Articles, ABA irresponsive, Pyrabactin, Sulfonamides, Pyr1, Chemistry, Arabidopsis Proteins, organic chemicals, fungi, food and beverages, Cell biology, 030104 developmental biology, 030220 oncology & carcinogenesis, Mutation, ABA independent, Research Article, Abscisic Acid, Signal Transduction |
| الوصف: | Abscisic acid (ABA) plays a vital role in many developmental processes and the response to adaptive stress in plants. Under drought stress, plants enhance levels of ABA and activate ABA receptors, but under harsh environmental stress, plants usually cannot efficiently synthesize and release sufficient quantities of ABA. The response of plants to harsh environmental stress may be improved through ABA‐independent activation of ABA receptors. The molecular basis of ABA‐independent inhibition of group A protein phosphatases type 2C (PP2Cs) by pyrabactin resistance/Pyr1‐like (PYR1/PYLs) is not yet clear. Here, we used our previously reported structures of PYL3 to first obtain the monomeric PYL3 mutant and then to introduce bulky hydrophobic residue substitutions to promote the closure of the Gate/L6/CL2 loop, thereby mimicking the conformation of ABA occupancy. Through structure‐guided mutagenesis and biochemical characterization, we investigated the mechanism of ABA‐independent activation of PYL3. Two types of PYL3 mutants were obtained: (a) PYL3 V108K V107L V192F can bind to ABA and effectively inhibit HAB1 without ABA; (b) PYL3 V108K V107F V192F, PYL3 V108K V107L V192F L111F and PYL3 V108K V107F V192F L111F cannot recognize ABA but can greatly inhibit HAB1 without ABA. Intriguingly, the ability of PYL3 mutants to bind to ABA was severely compromised if any two of three variable residues (V107, V192 and L111) were mutated into a bulky hydrophobic residue. The introduction of PYL3 mutants into transgenic plants will help elucidate the functionality of PYL3 in vivo and may facilitate the future production of transgenic crops with high yield and tolerance of abiotic stresses. PYL3 binds to abscisic acid (ABA) to inhibit the phosphatase activity of PP2Cs effectively. The molecular basis of ABA‐independent inhibition of PP2Cs by PYL3 is not yet clear. Here, we first obtain the monomeric PYL3 mutant and then introduce bulky hydrophobic residue substitutions to promote closure of the Gate/L6/CL2 loop. Four PYL3 mutants can greatly inhibit PP2Cs without ABA. |
| اللغة: | English |
| تدمد: | 2211-5463 |
| URL الوصول: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::29ddac7fc4a504e2e225c6819c1d9b06 http://europepmc.org/articles/PMC8091583 |
| حقوق: | OPEN |
| رقم الأكسشن: | edsair.doi.dedup.....29ddac7fc4a504e2e225c6819c1d9b06 |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 22115463 |
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