Functional domain analysis of the Remorin protein LjSYMREM1 in Lotus japonicus.

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 essent...

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Autores principales:	Katalin Tóth, Thomas F Stratil, Esben B Madsen, Juanying Ye, Claudia Popp, Meritxell Antolín-Llovera, Christina Grossmann, Ole N Jensen, Arthur Schüssler, Martin Parniske, Thomas Ott
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2012
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/9235ea3c32184653b9b59e43b734704d
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spelling	oai:doaj.org-article:9235ea3c32184653b9b59e43b734704d2021-11-18T07:29:31ZFunctional domain analysis of the Remorin protein LjSYMREM1 in Lotus japonicus.1932-620310.1371/journal.pone.0030817https://doaj.org/article/9235ea3c32184653b9b59e43b734704d2012-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/22292047/pdf/?tool=EBIhttps://doaj.org/toc/1932-6203In 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.Katalin TóthThomas F StratilEsben B MadsenJuanying YeClaudia PoppMeritxell Antolín-LloveraChristina GrossmannOle N JensenArthur SchüsslerMartin ParniskeThomas OttPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 7, Iss 1, p e30817 (2012)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Katalin Tóth Thomas F Stratil Esben B Madsen Juanying Ye Claudia Popp Meritxell Antolín-Llovera Christina Grossmann Ole N Jensen Arthur Schüssler Martin Parniske Thomas Ott Functional domain analysis of the Remorin protein LjSYMREM1 in Lotus japonicus.
description	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.
format	article
author	Katalin Tóth Thomas F Stratil Esben B Madsen Juanying Ye Claudia Popp Meritxell Antolín-Llovera Christina Grossmann Ole N Jensen Arthur Schüssler Martin Parniske Thomas Ott
author_facet	Katalin Tóth Thomas F Stratil Esben B Madsen Juanying Ye Claudia Popp Meritxell Antolín-Llovera Christina Grossmann Ole N Jensen Arthur Schüssler Martin Parniske Thomas Ott
author_sort	Katalin Tóth
title	Functional domain analysis of the Remorin protein LjSYMREM1 in Lotus japonicus.
title_short	Functional domain analysis of the Remorin protein LjSYMREM1 in Lotus japonicus.
title_full	Functional domain analysis of the Remorin protein LjSYMREM1 in Lotus japonicus.
title_fullStr	Functional domain analysis of the Remorin protein LjSYMREM1 in Lotus japonicus.
title_full_unstemmed	Functional domain analysis of the Remorin protein LjSYMREM1 in Lotus japonicus.
title_sort	functional domain analysis of the remorin protein ljsymrem1 in lotus japonicus.
publisher	Public Library of Science (PLoS)
publishDate	2012
url	https://doaj.org/article/9235ea3c32184653b9b59e43b734704d
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Functional domain analysis of the Remorin protein LjSYMREM1 in Lotus japonicus.

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