5 results on '"wak1"'
Search Results
2. In vitro characterization of the homogalacturonan-binding domain of the wall-associated kinase WAK1 using site-directed mutagenesis
- Author
-
Decreux, Annabelle, Thomas, Annick, Spies, Benoît, Brasseur, Robert, Cutsem, Pierre Van, and Messiaen, Johan
- Subjects
- *
ARABIDOPSIS , *ARABIDOPSIS thaliana , *ORGANIC acids , *LEAVENING agents - Abstract
Abstract: Wall-associated kinase 1 – WAK1 is a transmembrane protein containing a cytoplasmic Ser/Thr kinase domain and an extracellular domain in contact with the pectin fraction of the plant cell wall in Arabidopsis thaliana (L.) HEYNH. In a previous paper [Decreux, A., Messiaen, J., 2005. Wall-associated kinase WAK1 interacts with cell wall pectins in a calcium-induced conformation. Plant Cell Physiol. 46, 268–278], we showed that a recombinant peptide expressed in yeast corresponding to amino acids 67–254 of the extracellular domain of WAK1 specifically interacts with commercial non-methylesterified homogalacturonic acid, purified homogalacturonans from Arabidopsis and oligogalacturonides in a calcium-induced conformation. In this report, we used a receptor binding domain sequence-based prediction method to identify four putative binding sites in the extracellular domain of WAK1, in which cationic amino acids were selected for substitution by site-directed mutagenesis. Interaction studies between mutated forms of WAK1 and homogalacturonans allowed us to identify and confirm at least five specific amino acids involved in the interaction with homogalacturonan dimers and multimers. The presence of this homogalacturonan-binding domain within the extracellular domain of WAK1 is discussed in terms of cell wall architecture and signal transduction. [Copyright &y& Elsevier]
- Published
- 2006
- Full Text
- View/download PDF
3. Oxygen-evolving enhancer protein 2 is phosphorylated by glycine-rich protein 3/wall-associated kinase 1 in Arabidopsis
- Author
-
Yang, Eun Ju, Oh, Young Ah, Lee, Eui Seung, Park, Ae Ran, Cho, Somi K., Yoo, Yung Joon, and Park, Ohkmae K.
- Subjects
- *
ARABIDOPSIS , *CELL membranes - Abstract
The Arabidopsis wall-associated receptor kinase, WAK1, is a member of WAK family that links the plasma membrane to the extracellular matrix. A glycine-rich secreted protein, AtGRP-3, was previously shown to regulate WAK1 functions through binding to the extracellular domain of WAK1. In this study, we sought to determine the downstream molecules of the AtGRP-3/WAK1 signaling pathway, by using two-dimensional gel electrophoresis combined with Edman sequencing and matrix-assisted laser desorption/ionization-time-of-flight mass spectrometry (MALDI-TOF MS). We report here that a chloroplast protein, oxygen-evolving enhancer protein 2 (OEE2), specifically interacts with the cytoplasmic kinase domain of WAK1 and becomes phosphorylated in an AtGRP-3-dependent manner. The phosphorylation of OEE2 is also induced in Arabidopsis by treatment with avirulent Pseudomonas syringae. Taken together, these results suggest that OEE2 activity is regulated by AtGRP-3/WAK1. [Copyright &y& Elsevier]
- Published
- 2003
- Full Text
- View/download PDF
4. In silico study of wall-associated kinase family reveals large-scale genomic expansion potentially connected with functional diversification in Populus
- Author
-
Jean-Louis Julien, Beatriz Muries, Stéphane Maury, Boris Fumanal, Daniel Auguin, Sylvain Bourgerie, Kévin Tocquard, David Lopez, Jean-Stéphane Venisse, Clément Lafon-Placette, Jérôme Franchel, Philippe Label, Patricia Roeckel-Drevet, Gisèle Bronner, Laboratoire de Physique et Physiologie Intégratives de l'Arbre Fruitier et Forestier (PIAF), Institut National de la Recherche Agronomique (INRA)-Université Blaise Pascal - Clermont-Ferrand 2 (UBP), USC 1328 (ARCHE), Institut National de la Recherche Agronomique (INRA), Laboratoire de Biologie des Ligneux et des Grandes Cultures (LBLGC), Institut National de la Recherche Agronomique (INRA)-Université d'Orléans (UO), Laboratoire Microorganismes : Génome et Environnement (LMGE), Université Blaise Pascal - Clermont-Ferrand 2 (UBP)-Université d'Auvergne - Clermont-Ferrand I (UdA)-Centre National de la Recherche Scientifique (CNRS), LBLGC, Université d'Orléans (UO), and Université Blaise Pascal - Clermont-Ferrand 2 (UBP)-Centre National de la Recherche Scientifique (CNRS)-Université d'Auvergne - Clermont-Ferrand I (UdA)
- Subjects
Populus trichocarpa ,In silico ,Protein domain ,protein-kinase ,Computational biology ,Horticulture ,Microarray data mining ,Phylogenetics ,Arabidopsis ,Botany ,receptor kinase ,expression ,Genetics ,phylogénie ,Gene family ,[SDV.BV]Life Sciences [q-bio]/Vegetal Biology ,Molecular Biology ,evolutionary expansion ,Phylogeny ,stress abiotique ,Wall-Associated Kinase ,Vegetal Biology ,Phylogenetic tree ,biology ,Abiotic biotic stress ,Forestry ,WAK ,Populus ,gene family ,maximum-likelihood ,arabidopsis ,poplar ,wak1 ,transcriptome ,biology.organism_classification ,analyse microarray ,biology.protein ,Biologie végétale - Abstract
MECA; The wall-associated kinases (WAKs) are a family of transmembrane proteins involved in pathogen responses and cell elongation in Arabidopsis. They belong to the major receptor-like kinase (RLK) family in plants. Given their architecture and connection to the cell wall, WAKs are thought to perceive and propagate extracellular signals. This study reports the characterization of the WAK family in a woody species based on the v3.0 genome assembly of Populus trichocarpa. In silico analysis revealed a total of 175 PtWAK sequences classified into four groups based on protein domains. Of the PtWAKs, 91.5 % were found in tandem-duplicated clusters contributing to the expansion of the family in poplar. Microarray and EST expression data mining revealed contrasting temporal and spatial expression patterns in stress treatments for several WAK members. The WAKs in poplar form the largest WAK family encountered to date in plants. The combination of phylogenetic and transcriptional data showed that members in nonexpanded clusters were mainly expressed in developmental processes, whereas PtWAKs that had evolved independently in a species-specific way were structured in clusters and were involved in resistance responses. This paper offers an overview of WAK family structure in P. trichocarpa, which will be useful for further functional analysis of the PtWAK family.
- Published
- 2014
- Full Text
- View/download PDF
5. Arabidopsis L-type lectin receptor kinases: phylogeny, classification, and expression profiles
- Author
-
Klaas Bouwmeester and Francine Govers
- Subjects
Physiology ,Molecular Sequence Data ,protein-kinase ,Arabidopsis ,Plant Science ,perception ,Protein Serine-Threonine Kinases ,Genome ,Gene Expression Regulation, Plant ,evolution ,Arabidopsis thaliana ,Gene family ,thaliana ,wall ,Amino Acid Sequence ,Gene ,Peptide sequence ,Phylogeny ,Genetics ,biology ,EPS-2 ,Arabidopsis Proteins ,CD69 ,extracellular domain ,Gene Expression Regulation, Developmental ,biology.organism_classification ,Laboratorium voor Phytopathologie ,wak1 ,Gene nomenclature ,s-locus ,Multigene Family ,Laboratory of Phytopathology ,gene family ,identification ,Sequence Alignment - Abstract
In plants, lectin receptor kinases are considered to play crucial roles during development and in the adaptive response to various stimuli. Arabidopsis lectin receptor kinases can be divided into three type-classes based on sequence similarity of their extracellular lectin motifs. The current study focuses on the legume-like lectin receptor kinases (LecRKs), which are regarded as ideal candidates for monitoring cell wall integrity and are possibly functional in adaptive responses. An inventory of the Arabidopsis LecRK gene family is presented here. It consists of 45 members including three that were recently identified; two encode N-terminal truncated variants one of which has two in tandem kinase domains. Phylogenetic trees derived from full-length amino acid sequence alignments were highly concordant to phylograms that were purely based on lectin motifs or kinase domains. The phylograms allowed reclassification of the LecRK genes and hence a new proposal for gene nomenclature was suggested. In addition, a comprehensive expression analysis was executed by exploring public repositories. This revealed that several LecRK genes are differentially expressed during plant growth and development. Moreover, multiple LecRKs appear to be induced upon treatment with elicitors and pathogen infection. Variation in gene expression was also analysed in seedlings of diverse Arabidopsis accessions. Taken together, this study provides a genome-wide overview of the LecRK gene family and an up-to-date classification using a novel and systematic gene nomenclature.
- Published
- 2009
Catalog
Discovery Service for Jio Institute Digital Library
For full access to our library's resources, please sign in.