Abstract
Rho GTPases activating protein 2 (RGA2) is primarily involved in the modulation of numerous morphological events in eukaryotes. It protects plants by triggering the defense system which restricts the pathogen growth. This is the first report on the isolation, purification and characterization of RGA2 from the stems of Tinospora cordifolia, a medicinal plant. The RGA2 was purified using simple two-step process using DEAE-Hi-Trap FF and Superdex 200 chromatography columns, with a high yield. The purity of RGA2 was confirmed by SDS-PAGE and identified by MALDI-TOF/MS. The purified protein was further characterized for its secondary structural elements using the far-UV circular dichroism measurements. Our purification procedure is simple two-step process with high yield which can be further used to produce RGA2 for structural and functional studies.Electronic supplementary materialThe online version of this article (doi:10.1007/s13205-016-0400-3) contains supplementary material, which is available to authorized users.
Highlights
The Rho GTPases activating protein 2 (RGA2), belonging to the superfamily of small G proteins, is found in both higher and lower eukaryotic organisms
RGA2 protein contains leucine-rich repeat (LRR) domains which are involved in diverse biological processes including signal transduction, cell adhesion and the innate immune response
For the first time we are reporting a simplified procedure for the purification of RGA2 from green stems of Tinospora cordifolia
Summary
The Rho GTPases activating protein 2 (RGA2), belonging to the superfamily of small G proteins, is found in both higher and lower eukaryotic organisms. These regulators modify the signaling activity of the GTPase (de Bettignies et al 2001)
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