Publications by authors named "Reidunn Birgitta Aalen"

3 Publications

  • Page 1 of 1

In Silico Prediction of Ligand-Binding Sites of Plant Receptor Kinases Using Conservation Mapping.

Methods Mol Biol 2017 ;1621:93-105

Section for Genetics and Evolutionary Biology, Department of Biosciences, University of Oslo, Oslo, Norway.

Plasma membrane-bound plant receptor-like kinases (RLKs) can be categorized based on their ligand-binding extracellular domain. The largest group encompasses RLKs having ectodomains with leucine-rich repeats (LRRs). The LRR-RLKs can further be assigned to classes mainly based on the number of LRRs. Many of the receptors of the classes X and XI with more than 20 LRRs are activated by small secreted peptide ligands. To understand how peptide signaling works, it is of interest to identify the amino acids of the receptor that are directly involved in ligand interaction. Such residues have most likely been conserved over evolutionary time and can therefore be predicted to be conserved in receptor orthologues of different plant species. Here we present an in silico method to identify such residues. This involves a simplified method for identification of orthologues and a web-based program for identifying the most conserved amino acids aside from the leucines that structure the ectodomain. The method has been validated for the LRR-RLKs HAESA (HAE) and PHYTOSULFOKINE RECEPTOR1 (PSKR1) for which conservation-mapping results closely matched recent structure-based identification of ligand and co-receptor-interacting residues.
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http://dx.doi.org/10.1007/978-1-4939-7063-6_9DOI Listing
March 2018

Maturing peptides open for communication.

J Exp Bot 2013 Dec;64(17):5231-5

Department of Biosciences, University of Oslo, Norway.

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http://dx.doi.org/10.1093/jxb/ert378DOI Listing
December 2013

SET domain proteins in plant development.

Biochim Biophys Acta 2011 Aug 23;1809(8):407-20. Epub 2011 May 23.

Department of Molecular Biosciences, University of Oslo, Oslo, Norway.

Post-translational methylation of lysine residues on histone tails is an epigenetic modification crucial for regulation of chromatin structure and gene expression in eukaryotes. The majority of the histone lysine methyltransferases (HKMTases) conferring such modifications are proteins with a conserved SET domain responsible for the enzymatic activity. The SET domain proteins in the model plant Arabidopsis thaliana can be assigned to evolutionarily conserved classes with different specificities allowing for different outcomes on chromatin structure. Here we review the present knowledge of the biochemical and biological functions of plant SET domain proteins in developmental processes. This article is part of a Special Issue entitled: Epigenetic control of cellular and developmental processes in plants.
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http://dx.doi.org/10.1016/j.bbagrm.2011.05.008DOI Listing
August 2011
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