Differential gel electrophoresis (DIGE) to quantitatively monitor early symbiosis- and pathogenesis-induced changes of the Medicago truncatula root proteome

authored by

Leif Schenkluhn, Natalija Hohnjec, Karsten Niehaus, Udo Schmitz, Frank Colditz

Abstract

Symbiosis- and pathogenesis-related early protein induction patterns in the model legume Medicago truncatula were analysed with two-dimensional differential gel electrophoresis. Two symbiotic soil microorganisms (Glomus intraradices, Sinorhizobium meliloti) were used in single infections and in combination with a secondary pathogenic infection by the oomycete Aphanomyces euteiches. Proteomic analyses performed 6 and 24 h after inoculations led to identification of 87 differentially induced proteins which likely represent the M. truncatula root 'interactome'. A set of proteins involved in a primary antioxidant defense reaction was detected during all associations investigated. Symbiosis-related protein induction includes a typical factor of early symbiosis-specific signalling (CaM-2), two Ran-binding proteins of nucleocytoplasmic signalling, and a set of energy-related enzymes together with proteins involved in symbiosis-initiated C- and N-fixation. Pathogen-associated protein induction consists of mainly PR proteins, Kunitz-type proteinase inhibitors, a lectin, and proteins related to primary carbohydrate metabolism and phytoalexin synthesis. Absence of PR proteins and decreased pathogen-induced protein patterns during mixed symbiotic and pathogenic infections indicate bioprotective effects due to symbiotic co-infection. Several 14-3-3 proteins were found as predominant proteins during mixed infections. With respect to hormone-regulation, A. euteiches infection led to induction of ABA-related pathways, while auxin-related pathways are induced during symbiosis.

Organisation(s)

Section Plant Genomics
Section Plant Molecular Biology and Plant Proteomics

External Organisation(s)

Bielefeld University

Type

Article

Journal

Journal of Proteomics

Volume

73

Pages

753-768

No. of pages

16

ISSN

1874-3919

Publication date

03.11.2009

Publication status

Published

Peer reviewed

Yes

ASJC Scopus subject areas

Biophysics, Biochemistry

Electronic version(s)

https://doi.org/10.1016/j.jprot.2009.10.009 (Access: Unknown)