Molecular docking analysis of ahl molecule on plant protein arr10

Abstract

In rhizosphere Plant Growth Promoting Rhizobacteria (PGPR) produce N-acyl-l-homoserine lactones (AHL) as the quorum-sensing (QS) signals. AHLs can act as trans-kingdom signalling molecules between plants and rhizobacteria and that can regulate plant growth and development. The plant-beneficial PGPR Burkholderia phytofirmans PsJN promotes growth in Arabidopsis thaliana by producing 3-oxo-dodecanoyl homoserine lactone (oxo-C14-HSL) from their quorum-sensing (QS) system. In bacteria, QS system functions by binding AHL to the LuxR-family of sensor/regulator proteins through their response regulator receiver domain. It has been hypothesized that by using similar response domain, Arabidopsis response regulator 10 (ARR10) proteins may act as binding site for 3-oxo-dodecanoyl homoserine lactone. ARRs are involved in cytokinin signalling pathways and thus these types of lactones can regulate growth in Arabidopsis. We prove the binding of oxo-C14-HSL with ARR10 by using molecular docking technique and analysing the docking result.