Prof. Schmitz-Linneweber erforscht die Genregulation in Chloroplasten und Mitochondrien, insbesondere wie RNA-bindende Proteine (sogenannte Ribonukleoproteine) die Stabilität und Verarbeitung von RNA steuern und damit die Photosynthese und Energieproduktion in Pflanzen regulieren. Aktuell konzentriert er sich auf die Rolle dieser Proteine bei der Anpassung an Kältestress und auf die Mechanismen der RNA-Verarbeitung in fragmentierten Mitochondrien von Parasiten wie Toxoplasma. Seine Erkenntnisse ermöglichen ein tieferes Verständnis der Stresstoleranz von Pflanzen und könnten langfristig zu robusteren Nutzpflanzen führen; zudem liefern die Arbeiten zu parasitären Mitochondrien Ansatzpunkte für die Parasitologie und Infektionsforschung.
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Prof. Dr. Christian Schmitz-Linneweber
HU-FIS-Profil ↗Validating C. Elegans Healthspan Model for Better Understanding Factors Causing Health and Disease, to Develop Evidence Based Prevention, Diagnostic, Therapeutic and Other Strategies
company
Validating C. Elegans Healthspan Model for Better Understanding Factors Causing Health and Disease, to Develop Evidence Based Prevention, Diagnostic, Therapeutic and Other Strategies
company
Validating C. Elegans Healthspan Model for Better Understanding Factors Causing Health and Disease, to Develop Evidence Based Prevention, Diagnostic, Therapeutic and Other Strategies
other
IGRK 2290: Grenzen überwinden: Molekulare Interaktionen bei Malaria
university
Die Erforschung der plastidären GNATs: Acetylierung als Regulationsmechanismus in der Photosynthese und Seneszenz (AcetylPlast)
other
IGRK 2290/1: Grenzen überwinden: Molekulare Interaktionen bei Malaria
university
Förderer: DFG Nachwuchsgruppe Zeitraum: 11/2005 - 06/2009 Projektleitung: Prof. Dr. Christian Schmitz-Linneweber
Förderer: DFG Nachwuchsgruppe Zeitraum: 11/2007 - 10/2009 Projektleitung: Prof. Dr. Christian Schmitz-Linneweber
Förderer: DFG Sonderforschungsbereich Zeitraum: 01/2008 - 12/2010 Projektleitung: Prof. Dr. Christian Schmitz-Linneweber
Trends in Plant Science · DOI
Molecular Biology and Evolution · DOI
Pentatricopeptide repeat (PPR) proteins form a huge family in plants (450 members in Arabidopsis and 477 in rice) defined by tandem repetitions of characteristic sequence motifs. Some of these proteins have been shown to play a role in posttranscriptional processes within organelles, and they are thought to be sequence-specific RNA-binding proteins. The origins of this family are obscure as they are lacking from almost all prokaryotes, and the spectacular expansion of the family in land plants is equally enigmatic. In this study, we investigate the growth of the family in plants by undertaking a genome-wide identification and comparison of the PPR genes of 3 organisms: the flowering plants Arabidopsis thaliana and Oryza sativa and the moss Physcomitrella patens. A large majority of the PPR genes in each of the flowering plants are intron less. In contrast, most of the 103 PPR genes in Physcomitrella are intron rich. A phylogenetic comparison of the PPR genes in all 3 species shows similarities between the intron-rich PPR genes in Physcomitrella and the few intron-rich PPR genes in higher plants. Intron-poor PPR genes in all 3 species also display a bias toward a position of their introns at their 5' ends. These results provide compelling evidence that one or more waves of retrotransposition were responsible for the expansion of the PPR gene family in flowering plants. The differing numbers of PPR proteins are highly correlated with differences in organellar RNA editing between the 3 species.
The Plant Cell · DOI
The pentatricopeptide repeat (PPR) is a degenerate 35-amino acid repeat motif that is widely distributed among eukaryotes. Genetic, biochemical, and bioinformatic data suggest that many PPR proteins influence specific posttranscriptional steps in mitochondrial or chloroplast gene expression and that they may typically bind RNA. However, biological functions have been determined for only a few PPR proteins, and with few exceptions, substrate RNAs are unknown. To gain insight into the functions and substrates of the PPR protein family, we characterized the maize (Zea mays) nuclear gene ppr4, which encodes a chloroplast-targeted protein harboring both a PPR tract and an RNA recognition motif. Microarray analysis of RNA that coimmunoprecipitates with PPR4 showed that PPR4 is associated in vivo with the first intron of the plastid rps12 pre-mRNA, a group II intron that is transcribed in segments and spliced in trans. ppr4 mutants were recovered through a reverse-genetic screen and shown to be defective for rps12 trans-splicing. The observations that PPR4 is associated in vivo with rps12-intron 1 and that it is also required for its splicing demonstrate that PPR4 is an rps12 trans-splicing factor. These findings add trans-splicing to the list of RNA-related functions associated with PPR proteins and suggest that plastid group II trans-splicing is performed by different machineries in vascular plants and algae.