Prof. Dr. Christian Schmitz-Linneweber

Profil

Zusammenfassung

Christian Schmitz-Linneweber erforscht die Genexpression in Chloroplasten und Mitochondrien von Pflanzen, insbesondere die Rolle von RNA-bindenden Proteinen bei der Regulierung, Stabilisierung und Verarbeitung von Organellen-RNAs. Seine Expertise umfasst die molekularen Mechanismen, wie Pflanzen ihre Photosynthese und Energieproduktion unter wechselnden Bedingungen anpassen – ein Wissen, das für die Entwicklung stressresistenterer Nutzpflanzen relevant ist.

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Name

Prof. Dr. Christian Schmitz-Linneweber

Titel

Prof. Dr.

Fakultät

Lebenswissenschaftliche Fakultät

Institut

Institut für Biologie

Arbeitsgruppe

Molekulare Genetik

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HU-FIS-Profil

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Zuletzt gescrapt

28.6.2026, 01:12:36

• Analyse der Aktivierung plastidärer Translation und RNA-Stabilisierung durch PPR-Proteine und PPR-induzierte sRNAs

  Quelle ↗

  Förderer: DFG Sachbeihilfe Zeitraum: 08/2013 - 09/2016 Projektleitung: Prof. Dr. Christian Schmitz-Linneweber

• Analyse von Pentatricopeptide repeat Proteinen in vivo: Ziel-RNAs und Funktionen III

  Quelle ↗

  Förderer: DFG Nachwuchsgruppe Zeitraum: 11/2009 - 09/2011 Projektleitung: Prof. Dr. Christian Schmitz-Linneweber

• Chloroplastidäre Ribonukleoproteine: Stabilitätsgeber für chloroplastidäre RNAs während Stressantworten

  Quelle ↗

  Förderer: DFG Sachbeihilfe Zeitraum: 09/2015 - 08/2018 Projektleitung: Prof. Dr. Christian Schmitz-Linneweber

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• Pentatricopeptide repeat proteins: a socket set for organelle gene expression

  2008

  Trends in Plant Science · 833 Zitationen · DOI

• On the Expansion of the Pentatricopeptide Repeat Gene Family in Plants

  2008

  Molecular Biology and Evolution · 400 Zitationen · 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.

• A Pentatricopeptide Repeat Protein Facilitates the <i>trans-</i>Splicing of the Maize Chloroplast <i>rps12</i> Pre-mRNA

  2006

  The Plant Cell · 301 Zitationen · 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.

• Abiomics Europe KFT

  Validating C. Elegans Healthspan Model for Better Understanding Factors Causing Health and Disease, to Develop Evidence Based Prevention, Diagnostic, Therapeutic and Other Strategies

  company

• AnalytiCon Discovery GmbH

  Validating C. Elegans Healthspan Model for Better Understanding Factors Causing Health and Disease, to Develop Evidence Based Prevention, Diagnostic, Therapeutic and Other Strategies

  company

• Australian National University

  IGRK 2290: Grenzen überwinden: Molekulare Interaktionen bei Malaria

  university