Characterization of anArabidopsis thalianaGene that Defines a New Class of Putative Plant Receptor Kinases with an Extracellular Lectin-like Domain

Hervé, Christine; Dabos, Patrick; Galaud, Jean‐Philippe; Rougé, Pierre; Lescure, Bernard

doi:10.1006/jmbi.1996.0286

Cited by 136 publications

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“…In this paper, we have tested the hypothesis (Hervé et al, 1996;Hirsch, 1999) that LecRKs may play a role in the legume-rhizobia symbiosis. Screening of cDNA libraries and examination of M. truncatula EST banks has shown that the model legume contains at least nine LecRK genes.…”

Section: Discussionmentioning

confidence: 99%

“…Roots expressing this fusion protein however showed an increase in nodule number, suggesting that expression of MtLecRK1;1 influences nodulation. The potential role of LecRKs in the legumerhizobia symbiosis is discussed.The lectin-like receptor kinases (LecRKs) are a class of proteins originally described from Arabidopsis (Hervé et al, 1996). They have a structure similar to other plant receptor-like kinases (RLKs; Shiu and Bleecker, 2001;Cock et al, 2002) with an N-terminal targeting signal, a presumably extracellular domain, a single transmembrane (TM)-spanning helix, and a cytosolic kinase domain.…”

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confidence: 99%

“…The Arabidopsis genome contains at least 42 LecRK sequences that have been grouped into three classes (A-C) plus an additional nine sequences of related soluble lectins (Barre et al, 2002). Searches in plant databases reveal that LecRK genes are widespread in higher plants, but apart from Arabidopsis (Hervé et al, 1996, Riou et al, 2002, LecRK genes have been studied only in lombardy poplar (Populus nigra var italica; Nishiguchi et al, 2002). RLK genes with legume lectin-like domains are not found in the complete genome sequences of yeast (Saccharomyces cerevisiae) or human (Homo sapiens).…”

mentioning

confidence: 99%

“…The structure of LecRKs has led to suggestions that in legumes they could be involved in the legumerhizobia symbiosis (Hervé et al, 1996;Hirsch, 1999). The establishment of this symbiosis requires at least two types of rhizobial saccharidic signals.…”

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confidence: 99%

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Characterization of Four Lectin-Like Receptor Kinases Expressed in Roots of Medicago truncatula. Structure, Location, Regulation of Expression, and Potential Role in the Symbiosis with Sinorhizobium meliloti

et al. 2003

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To study the role of LecRK (lectin-like receptor kinase) genes in the legume-rhizobia symbiosis, we have characterized the four Medicago truncatula Gaernt. LecRK genes that are most highly expressed in roots. Three of these genes, MtLecRK7;1, MtLecRK7;2, and MtLecRK7;3, encode proteins most closely related to the Class A LecRKs of Arabidopsis, whereas the protein encoded by the fourth gene, MtLecRK1;1, is most similar to a Class B Arabidopsis LecRK. All four genes show a strongly enhanced root expression, and detailed studies on MtLecRK1;1 and MtLecRK7;2 revealed that the levels of their mRNAs are increased by nitrogen starvation and transiently repressed after either rhizobial inoculation or addition of lipochitooligosaccharidic Nod factors. Studies of the MtLecRK1;1 and MtLecRK7;2 proteins, using green fluorescent protein fusions in transgenic M. truncatula roots, revealed that they are located in the plasma membrane and that their central transmembrane-spanning helix is required for correct sorting. Moreover, their lectin-like domains appear to be highly glycosylated. Of the four proteins, only MtLecRK1;1 shows a high conservation of key residues implicated in monosaccharide binding, and molecular modeling revealed that this protein may be capable of interacting with Nod factors. However, no increase in Nod factor binding was found in roots overexpressing a fusion in which the kinase domain of this protein had been replaced with green fluorescent protein. Roots expressing this fusion protein however showed an increase in nodule number, suggesting that expression of MtLecRK1;1 influences nodulation. The potential role of LecRKs in the legumerhizobia symbiosis is discussed.The lectin-like receptor kinases (LecRKs) are a class of proteins originally described from Arabidopsis (Hervé et al., 1996). They have a structure similar to other plant receptor-like kinases (RLKs; Shiu and Bleecker, 2001;Cock et al., 2002) with an N-terminal targeting signal, a presumably extracellular domain, a single transmembrane (TM)-spanning helix, and a cytosolic kinase domain. The Arabidopsis genome contains over 610 RLKs that have been shown to be monophylogenetic with respect to the kinase domain and most closely related to the fruitfly (Drosophila melanogaster) Pelle and related animal cytoplasmic kinases (Shiu and Bleecker, 2001). In cases in which they have been tested, these kinases have been shown to have specificity for phosphorylation on Ser/Thr residues (Shiu and Bleecker, 2001).The plant RLKs can be grouped into more than 21 structural classes based on their extracellular domains (Shiu and Bleecker, 2001). The LecRKs represent one such class in which the extracellular domain is related to legume lectins. The Arabidopsis genome contains at least 42 LecRK sequences that have been grouped into three classes (A-C) plus an additional nine sequences of related soluble lectins (Barre et al., 2002). Searches in plant databases reveal that LecRK genes are widespread in higher plants, but apart from Arabidopsis (Hervé et al., 1996,...

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Section: Discussionmentioning

confidence: 99%

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confidence: 99%

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confidence: 99%

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confidence: 99%

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Characterization of Four Lectin-Like Receptor Kinases Expressed in Roots of Medicago truncatula. Structure, Location, Regulation of Expression, and Potential Role in the Symbiosis with Sinorhizobium meliloti

et al. 2003

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“…The majority of the incorporated phosphates in CBP-BRI1-KD occurred in the area corresponding to the p-Ser standard, with a minor amount in p-Thr and none in p-Tyr. Thus BRI1 resembles CLV1 (Williams et al, 1997;Stone et al, 1998), RLK5 , Ath.lecRK1 (Herve et al, 1996), and SRK (Stein and Nasrallah, 1993) in its preference for Ser over Thr. However, other plant receptor-like kinases have either an equal propensity for autophosphorylation on Ser and Thr, i.e.…”

Section: Bri1 Encodes An Active Ser/thr Kinasementioning

confidence: 91%

Recombinant Brassinosteroid Insensitive 1 Receptor-Like Kinase Autophosphorylates on Serine and Threonine Residues and Phosphorylates a Conserved Peptide Motif in Vitro

Oh¹,

Ray²,

et al. 2000

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BRASSINOSTEROID-INSENSITIVE 1 (BRI1) encodes a putative Leucine-rich repeat receptor kinase in Arabidopsis that has been shown by genetic and molecular analysis to be a critical component of brassinosteroid signal transduction. In this study we examined some of the biochemical properties of the BRI1 kinase domain (BRI1-KD) in vitro, which might be important predictors of in vivo function. Recombinant BRI1-KD autophosphorylated on serine (Ser) and threonine (Thr) residues with p-Ser predominating. Matrix-assisted laser desorption/ionization mass spectrometry identified a minimum of 12 sites of autophosphorylation in the cytoplasmic domain of BRI1, including five in the juxtamembrane region (N-terminal to the catalytic KD), five in the KD (one each in sub-domains I and VIa and three in sub-domain VIII), and two in the carboxy terminal region. Five of the sites were uniquely identified (Ser-838, Thr-842, Thr-846, Ser-858, and Thr-872), whereas seven were localized on short peptides but remain ambiguous due to multiple Ser and/or Thr residues within these peptides. The inability of an active BRI1-KD to transphosphorylate an inactive mutant KD suggests that the mechanism of autophosphorylation is intramolecular. It is interesting that recombinant BRI1-KD was also found to phosphorylate certain synthetic peptides in vitro. To identify possible structural elements required for substrate recognition by BRI1-KD, a series of synthetic peptides were evaluated, indicating that optimum phosphorylation of the peptide required R or K residues at P Ϫ 3, P Ϫ 4, and P ϩ 5 (relative to the phosphorylated Ser at P ϭ 0).

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Oligosaccharide signaling of plant cells

Etzler

1998

J. Cell. Biochem.

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A variety of oligosaccharide signals have been identified that function in the regulation of plant development, defense, and other interactions of plants with the environment. Some of these oligosaccharides are produced by various pathogens or symbionts, whereas others are synthesized by the plant itself. This mini-review summarizes our present state of information on these oligosaccharide signals and provides an overview of approaches being used to identify receptors for these signals and gain an understanding of the mechanism(s) by which these signals activate downstream events. Possible biotechnological applications of future work in this field are also considered. J. Cell. Biochem. Suppls. 30/31:123-128, 1998. © 1998 Wiley-Liss, Inc.

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Characterization of anArabidopsis thalianaGene that Defines a New Class of Putative Plant Receptor Kinases with an Extracellular Lectin-like Domain

Cited by 136 publications

References 0 publications

Characterization of Four Lectin-Like Receptor Kinases Expressed in Roots of Medicago truncatula. Structure, Location, Regulation of Expression, and Potential Role in the Symbiosis with Sinorhizobium meliloti

Characterization of Four Lectin-Like Receptor Kinases Expressed in Roots of Medicago truncatula. Structure, Location, Regulation of Expression, and Potential Role in the Symbiosis with Sinorhizobium meliloti

Recombinant Brassinosteroid Insensitive 1 Receptor-Like Kinase Autophosphorylates on Serine and Threonine Residues and Phosphorylates a Conserved Peptide Motif in Vitro

Oligosaccharide signaling of plant cells

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