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Functional Domain Analysis of the Remorin Protein LjSYMREM1 in Lotus japonicus

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  • Katalin Tóth, Department of Genetics, University of Munich, Tyskland
  • Thomas F Stratil, Department of Genetics, University of Munich, Tyskland
  • Esben B Madsen, Danmark
  • Juanying Ye, Department of Biochemistry and Molecular Biology, University of Southern Denmark, Danmark
  • Claudia Popp, Department of Genetics, University of Munich, Tyskland
  • Meritxell Antolín-Llovera, Department of Genetics, University of Munich, Tyskland
  • Iris Christina Grossmann
  • ,
  • Ole N Jensen, Department of Biochemistry and Molecular Biology, University of Southern Denmark, Danmark
  • Arthur Schüßler, Department of Genetics, University of Munich, Tyskland
  • Martin Parniske, Department of Genetics, University of Munich, Tyskland
  • Thomas Ott, Department of Genetics, University of Munich, Tyskland
In legumes rhizobial infection during root nodule symbiosis (RNS) is controlled by a conserved set of receptor proteins and downstream components. MtSYMREM1, a protein of the Remorin family in Medicago truncatula, was shown to interact with at least three receptor-like kinases (RLKs) that are essential for RNS. Remorins are comprised of a conserved C-terminal domain and a variable N-terminal region that defines the six different Remorin groups. While both N- and C-terminal regions of Remorins belonging to the same phylogenetic group are similar to each other throughout the plant kingdom, the N-terminal domains of legume-specific group 2 Remorins show exceptional high degrees of sequence divergence suggesting evolutionary specialization of this protein within this clade. We therefore identified and characterized the MtSYMREM1 ortholog from Lotus japonicus (LjSYMREM1), a model legume that forms determinate root nodules. Here, we resolved its spatio-temporal regulation and showed that over-expression of LjSYMREM1 increases nodulation on transgenic roots. Using a structure-function approach we show that protein interactions including Remorin oligomerization are mainly mediated and stabilized by the Remorin C-terminal region with its coiled-coil domain while the RLK kinase domains transiently interact in vivo and phosphorylate a residue in the N-terminal region of the LjSYMREM1 protein in vitro. These data provide novel insights into the mechanism of this putative molecular scaffold protein and underline its importance during rhizobial infection.
OriginalsprogEngelsk
TidsskriftP L o S One
Vol/bind7
Nummer1
Sider (fra-til)e30817
Antal sider13
ISSN1932-6203
DOI
StatusUdgivet - 23 jan. 2012

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