title: Spatio-temporal patterning of arginyl-tRNA protein transferase (ATE) contributes to gametophytic development in a moss.
abstract: The importance of the arginyl-tRNA protein transferase (ATE), the enzyme mediating post-translation arginylation of proteins in the N-end rule degradation (NERD) pathway of protein stability, was analysed in Physcomitrella patens and compared to its known functions in other eukaryotes. We characterize ATE:GUS reporter lines as well as ATE mutants in P. patens to study the impact and function of arginylation on moss development and physiology. ATE protein abundance is spatially and temporally regulated in P. patens by hormones and light and is highly abundant in meristematic cells. Further, the amount of ATE transcript is regulated during abscisic acid signalling and downstream of auxin signalling. Loss-of-function mutants exhibit defects at various levels, most severely in developing gametophores, in chloroplast starch accumulation and senescence. Thus, arginylation is necessary for moss gametophyte development, in contrast to the situation in flowering plants. Our analysis further substantiates the conservation of the N-end rule pathway components in land plants and highlights lineage-specific features. We introduce moss as a model system to characterize the role of the NERD pathway as an additional layer of complexity in eukaryotic development.
authors.affiliation: Plant Biotechnology, Faculty of Biology, University of Freiburg, Schaenzlestr. 1, 79104, Freiburg, Germany.|Institute of Biology 3, Faculty of Biology, University of Freiburg, Schaenzlestr. 1, 79104, Freiburg, Germany.
authors.forename: Christian
authors.initials: C
authors.lastname: Schuessele
authors.affiliation: Plant Biotechnology, Faculty of Biology, University of Freiburg, Schaenzlestr. 1, 79104, Freiburg, Germany.|Institute of Biology 3, Faculty of Biology, University of Freiburg, Schaenzlestr. 1, 79104, Freiburg, Germany.
authors.forename: Sebastian N W
authors.initials: SN
authors.lastname: Hoernstein
authors.affiliation: Plant Biotechnology, Faculty of Biology, University of Freiburg, Schaenzlestr. 1, 79104, Freiburg, Germany.
authors.forename: Stefanie J
authors.initials: SJ
authors.lastname: Mueller
authors.affiliation: Cell Biology, Faculty of Biology, University of Freiburg, Schaenzlestr. 1, 79104, Freiburg, Germany.
authors.forename: Marta
authors.initials: M
authors.lastname: Rodriguez-Franco
authors.affiliation: Plant Biotechnology, Faculty of Biology, University of Freiburg, Schaenzlestr. 1, 79104, Freiburg, Germany.
authors.forename: Timo
authors.initials: T
authors.lastname: Lorenz
authors.affiliation: Plant Biotechnology, Faculty of Biology, University of Freiburg, Schaenzlestr. 1, 79104, Freiburg, Germany.
authors.forename: Daniel
authors.initials: D
authors.lastname: Lang
authors.affiliation: Institute of Biology 3, Faculty of Biology, University of Freiburg, Schaenzlestr. 1, 79104, Freiburg, Germany.
authors.forename: Gabor L
authors.initials: GL
authors.lastname: Igloi
authors.affiliation: Plant Biotechnology, Faculty of Biology, University of Freiburg, Schaenzlestr. 1, 79104, Freiburg, Germany.|FRIAS - Freiburg Institute for Advanced Studies, University of Freiburg, 79104, Freiburg, Germany.|BIOSS - Centre for Biological Signalling Studies, University of Freiburg, 79104, Freiburg, Germany.|TIP - Trinational Institute for Plant Research, Upper Rhine Valley, 79104, Freiburg, Germany.
authors.forename: Ralf
authors.initials: R
authors.lastname: Reski
mesh_terms: D019881:Aminoacyltransferases / Q000378:metabolism*; D017360:Arabidopsis / Q000378:metabolism; D019521:Body Patterning / Q000235:genetics; D019068:Bryopsida / Q000201:enzymology* / Q000235:genetics / Q000254:growth & development* / Q000648:ultrastructure; D002734:Chlorophyll / Q000378:metabolism; D002736:Chloroplasts / Q000378:metabolism / Q000648:ultrastructure; D018506:Gene Expression Regulation, Plant; D017343:Genes, Plant; D055993:Germ Cells, Plant / Q000254:growth & development*; D009154:Mutation / Q000235:genetics; D009928:Organ Specificity; D010641:Phenotype; D063245:Plant Development; D060888:Real-Time Polymerase Chain Reaction; D013213:Starch / Q000378:metabolism; D013347:Subcellular Fractions / Q000378:metabolism
chemical_list: D002734:Chlorophyll; D013213:Starch; D019881:Aminoacyltransferases; C019727:arginyltransferase
keywords: Arabidopsis thaliana; N-end rule degradation (NERD); N-end rule pathway; Physcomitrella patens; arginyl-tRNA protein transferase (ATE); development; post-translational protein modification; starch accumulation