Local and Systemic Proteomic Changes in Medicago Truncatula at an Early Phase of Sinorhizobium meliloti Infection
journal contributionposted on 07.02.2014, 00:00 by Barbara Molesini, Daniela Cecconi, Youry Pii, Tiziana Pandolfini
A symbiotic association with N-fixing bacteria facilitates the growth of leguminous plants under nitrogen-limiting conditions. The establishment of the symbiosis requires signal exchange between the host and the bacterium, which leads to the formation of root nodules, inside which bacteria are hosted. The formation of nodules is controlled through local and systemic mechanisms, which involves root-shoot communication. Our study was aimed at investigating the proteomic changes occurring in shoots and concomitantly in roots of Medicago truncatula at an early stage of Sinorhizobium meliloti infection. The principal systemic effects consisted in alteration of chloroplast proteins, induction of proteins responsive to biotic stress, and changes in proteins involved in hormonal signaling and metabolism. The most relevant local effect was the induction of proteins involved in the utilization of photosynthates and C-consuming processes (such as sucrose synthase and fructose-bisphosphate aldolase). In addition, some redox enzymes such as peroxiredoxin and ascorbate peroxidase showed an altered abundance. The analysis of local and systemic proteome changes suggests the occurrence of a stress response in the shoots and the precocious alteration of energy metabolism in roots and shoots. Furthermore, our data indicate the possibility that ABA and ethylene participate in the communicative network between root and shoot in the control of rhizobial infection.
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Sinorhizobium meliloti InfectionAsucrose synthasestress responsealterationbacteriasignal exchangeroot nodulesinductionformationbiotic stressproteome changesrhizobial infectionSystemic Proteomic ChangesMedicago truncatulachloroplast proteinsSinorhizobium meliloti infectionenergy metabolismABAredox enzymesMedicago Truncatulaproteomic changesascorbate peroxidase