Molecular details of secretory phospholipase A2 from flax (Linum usitatissimum L.) provide insight into its structure and function

Payal Gupta, Prasanta K. Dash
2017 Scientific Reports  
Secretory phospholipase A 2 (sPLA 2 ) are low molecular weight proteins (12-18 kDa) involved in a suite of plant cellular processes imparting growth and development. With myriad roles in physiological and biochemical processes in plants, detailed analysis of sPLA 2 in flax/linseed is meagre. The present work, first in flax, embodies cloning, expression, purification and molecular characterisation of two distinct sPLA 2 s (I and II) from flax. PLA 2 activity of the cloned sPLA 2 s were
more » ... lly assayed authenticating them as bona fide phospholipase A 2 . Physiochemical properties of both the sPLA 2 s revealed they are thermostable proteins requiring di-valent cations for optimum activity.While, structural analysis of both the proteins revealed deviations in the amino acid sequence at C-& N-terminal regions; hydropathic study revealed LusPLA 2 I as a hydrophobic protein and LusPLA 2 II as a hydrophilic protein. Structural analysis of flax sPLA 2 s revealed that secondary structure of both the proteins are dominated by α-helix followed by random coils. Modular superimposition of LusPLA 2 isoforms with rice sPLA 2 confirmed monomeric structural preservation among plant phospholipase A 2 and provided insight into structure of folded flax sPLA 2 s. Published: xx xx xxxx OPEN www.nature.com/scientificreports/ 2 Scientific REPORtS | 7: 11080 |
doi:10.1038/s41598-017-10969-9 pmid:28894144 pmcid:PMC5593939 fatcat:y73nznmoobb7xlrxix2ojtguly