Filippo Passardi
University of Geneva
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Featured researches published by Filippo Passardi.
Plant Cell Reports | 2005
Filippo Passardi; Claudia Cosio; Claude Penel; Christophe Dunand
Plant peroxidases (class III peroxidases) are present in all land plants. They are members of a large multigenic family. Probably due to this high number of isoforms, and to a very heterogeneous regulation of their expression, plant peroxidases are involved in a broad range of physiological processes all along the plant life cycle. Due to two possible catalytic cycles, peroxidative and hydroxylic, peroxidases can generate reactive oxygen species (ROS) (•OH, HOO•), polymerise cell wall compounds, and regulate H2O2 levels. By modulating their activity and expression following internal and external stimuli, peroxidases are prevalent at every stage of plant growth, including the demands that the plant meets in stressful conditions. These multifunctional enzymes can build a rigid wall or produce ROS to make it more flexible; they can prevent biological and chemical attacks by raising physical barriers or by counterattacking with a large production of ROS; they can be involved in a more peaceful symbiosis. They are finally present from the first hours of a plant’s life until its last moments. Although some functions look paradoxical, the whole process is probably regulated by a fine-tuning that has yet to be elucidated. This review will discuss the factors that can influence this delicate balance.
Planta | 2006
Filippo Passardi; Michael Tognolli; Mireille De Meyer; Claude Penel; Christophe Dunand
Two class III peroxidases from Arabidopsis, AtPrx33 and Atprx34, have been studied in this paper. Their encoding genes are mainly expressed in roots; AtPrx33 transcripts were also found in leaves and stems. Light activates the expression of both genes in seedlings. Transformed seedlings producing AtPrx33-GFP or AtPrx34-GFP fusion proteins under the control of the CaMV 35S promoter exhibit fluorescence in the cell walls of roots, showing that the two peroxidases are localized in the apoplast, which is in line with their affinity for the Ca2+-pectate structure. The role they can play in cell wall was investigated using (1) insertion mutants that have suppressed or reduced expression of AtPrx33 or AtPrx34 genes, respectively, (2) a double mutant with no AtPrx33 and a reduced level of Atprx34 transcripts, (3) a mutant overexpressing AtPrx34 under the control of the CaMV 35S promoter. The major phenotypic consequences of these genetic manipulations were observed on the variation of the length of seedling roots. Seedlings lacking AtPrx33 transcripts have shorter roots than the wild-type controls and roots are still shorter in the double mutant. Seedlings overexpressing AtPrx34 exhibit significantly longer roots. These modifications of root length are accompanied by corresponding changes of cell length. The results suggest that AtPrx33 and Atprx34, two highly homologous Arabidopsis peroxidases, are involved in the reactions that promote cell elongation and that this occurs most likely within cell walls.
Journal of Experimental Botany | 2009
Michele Oliva; Grégory Theiler; Marcel Zamocky; Dominique Koua; Marcia Margis-Pinheiro; Filippo Passardi; Christophe Dunand
Peroxidases are enzymes that are implicated in several biological processes and are detected in all living organisms. The increasing number of sequencing projects and the poor quality of annotation justified the creation of an efficient tool that was suitable for collecting and annotating the huge quantity of data. Started in 2004 to collect only class III peroxidases, PeroxiBase has undergone important updates since then and, currently, the majority of peroxidase sequences from all kingdoms of life is stored in the database. In addition, the web site (http://peroxibase.isb-sib.ch) provides a series of bioinformatics tools and facilities suitable for analysing these stored sequences. In particular, the high number of isoforms in each organism makes phylogenetic studies extremely useful to elucidate the complex evolution of these enzymes, not only within the plant kingdom but also between the different kingdoms. This paper provides a general overview of PeroxiBase, focusing on its tools and the stored data. The main goal is to give researchers some guidelines to extract classified and annotated sequences from the data base in a quick and easy way in order to perform alignments and phylogenetic analysis. The description of the database is accompanied by the updates we have recently carried out in order to improve its completeness and make it more user-friendly.
Trends in Plant Science | 2004
Filippo Passardi; Claude Penel; Christophe Dunand
Phytochemistry | 2004
Filippo Passardi; David Longet; Claude Penel; Christophe Dunand
Phytochemistry | 2007
Filippo Passardi; Grégory Theiler; Marcel Zamocky; Claudia Cosio; Nicolas Rouhier; Felipe Teixera; Márcia Margis-Pinheiro; Vassilios Ioannidis; Claude Penel; Christophe Dunand
Phytochemistry | 2006
Nenad Bakalovic; Filippo Passardi; Vassilios Ioannidis; Claudia Cosio; Claude Penel; Christophe Dunand
Genomics | 2007
Filippo Passardi; Nenad Bakalovic; Felipe Karam Teixeira; Márcia Margis-Pinheiro; Claude Penel; Christophe Dunand
Gene | 2007
Filippo Passardi; Marcel Zamocky; Jocelyne Favet; Christa Jakopitsch; Claude Penel; Christian Obinger; Christophe Dunand
Journal of Plant Physiology | 2007
Filippo Passardi; Jan Dobias; Luisa Valério; Sonia Guimil; Claude Penel; Christophe Dunand