Structural and functional characterization of Solanum lycopersicum phosphatidylinositol 3-kinase C2 domain

Copyright © 2020 Elsevier Masson SAS. All rights reserved.

Bibliographische Detailangaben
Veröffentlicht in:Plant physiology and biochemistry : PPB. - 1991. - 148(2020) vom: 15. März, Seite 180-192
1. Verfasser: Pak Dek, Mohd Sabri (VerfasserIn)
Weitere Verfasser: Padmanabhan, Priya, Tiwari, Krishnaraj, Todd, James F, Paliyath, Gopinadhan
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2020
Zugriff auf das übergeordnete Werk:Plant physiology and biochemistry : PPB
Schlagworte:Journal Article C2 domain Membrane binding Phosphatidylinositol 3-kinase Senescence Phosphatidylinositol 3-Kinase EC 2.7.1.137
Beschreibung
Zusammenfassung:Copyright © 2020 Elsevier Masson SAS. All rights reserved.
Phosphatidylinositol 3-kinases (PI3Ks) are characterized by the presence of a C2 domain at the N-terminal end (class I, III); or at both the N-terminal and C-terminal ends (class II), sometimes including a Plextrin homology domain and/or a Ras domain. Plant PI3Ks are analogous to the class III mammalian PI3K. An N-terminal fragment (~170 aa) of the tomato PI3K regulatory domain including the C2 domain, was cloned and expressed in a bacterial system. This protein was purified to homogeneity and its physicochemical properties analyzed. The purified protein showed strong binding with monophosphorylated phosphatidylinositols, and the binding was dependent on calcium ion concentration and pH. In the overall tertiary structure of PI3K, C2 domain showed unique characteristics, having three antiparallel beta-sheets, hydrophobic regions, acidic as well as alkaline motifs, that can enable its membrane binding upon activation. To elucidate the functional significance of C2 domain, transgenic tobacco plants expressing the C2 domain of PI3K were generated. Transgenic plants showed defective pollen development and disrupted seed set. Flowers from the PI3K-C2 transgenic plants showed delayed wilting, and a decrease in ethylene production. It is likely that introduction of the PI3K-C2 segment may have interfered with the normal binding of PI3K to the membrane, delaying the onset of membrane lipid catabolism that lead to senescence
Beschreibung:Date Completed 13.04.2020
Date Revised 13.12.2023
published: Print-Electronic
Citation Status MEDLINE
ISSN:1873-2690
DOI:10.1016/j.plaphy.2020.01.014