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Identification of novel phosphatidic acid binding domain on sphingosine kinase 1 of Arabidopsis thaliana.

Authors
  • Pandit, Shatakshi1
  • Dalal, Vikram2
  • Mishra, Girish3
  • 1 - Department of Botany, University of Delhi, Delhi 110007, India. , (India)
  • 2 - Department of Biotechnology, Indian Institute of Technology, Roorkee, Uttarakhand 247667, India. , (India)
  • 3 - Department of Botany, University of Delhi, Delhi 110007, India. Electronic address: [email protected] , (India)
Type
Published Article
Journal
Plant physiology and biochemistry : PPB
Publication Date
May 08, 2018
Volume
128
Pages
178–184
Identifiers
DOI: 10.1016/j.plaphy.2018.04.039
PMID: 29783183
Source
Medline
Keywords
License
Unknown

Abstract

Phosphatidic acid (PA) is an important lipid signaling molecule which interacts with Arabidopsis thaliana Sphingosine kinase1 (AtSPHK1) during several abiotic stresses particularly drought stress as a result of Abscisic acid (ABA) signaling in guard cells. PA molecules respond by generating lipid signal and/or by binding and translocating target proteins to membrane. However, site of interaction and role of PA binding to AtSPHK1 is not clear yet. Owing to the importance of AtSPHK1 during stress signaling it is imperative to decipher the site of PA interaction with AtSPHK1. To identify the PA binding region of AtSPHK1, various deletion fragments from N-terminal and C-terminal region were prepared. Results from protein lipid overlay assay using various truncated proteins of AtSPHK1 suggested the involvement of N-terminal region, between 110 and 205 amino acids, in binding with PA. In-silico analyses performed to build homologous structure of AtSPHK1 revealed that PA docking occurs in the hydrophobic cavity of DAG-Kinase domain. Deletion of amino acids 182VSGDGI187 perturbed PA-AtSPHK1 binding, indicating an essential role of these six amino acids in PA-AtSPHK1 binding.

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