Reverse transcriptase activity of an intron encoded polypeptide.

Fassbender, S.; Brühl, K.H.; Ciriacy, Michael; Kück, Ulrich

doi:10.1002/j.1460-2075.1994.tb06482.x

Cited by 48 publications

(11 citation statements)

References 72 publications

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“…The gene confers ACR-toxin sensitivity to E. coli, and the mechanism of specificity in plants is alternative processing of the transcript of the gene conferring ACR-toxin sensitivity (Fig. This intron, known as a self-splicing group II intron, catalyses its own splicing (Leaver & Gray, 1982), and many of these introns have been reported to contain ORFs encoding polypeptides (Fassbender et al, 1994). For initial screening of the gene, mitochondrial DNA was isolated from rough lemon, and random BamHI fragments were expressed in E. coli, which is normally resistant to ACR-toxin.…”

Section: Acr-toxinmentioning

confidence: 99%

Host-selective toxins produced by the plant pathogenic fungusAlternaria alternata

et al. 2013

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Host-selective toxins (HSTs) produced by fungal plant pathogens are generally low-molecular-weight secondary metabolites with a diverse range of structures that function as effectors controlling pathogenicity or virulence in certain plant-pathogen interactions. There are now seven known diseases caused by Alternaria alternata in which HSTs are responsible for fungal pathogenesis. The pathogens have been defined as pathotypes of A. alternata because of morphological similarity but pathological differences. Chemical structures of HSTs from six pathotypes have been determined. The role of A. alternata HSTs in pathogenesis has been studied extensively, and discovery of the release of HSTs from germinating conidia prior to penetration aids in understanding the early participation of HSTs to induce susceptibility of host cells by suppressing their defence reactions. Many attempts have been made to find the target sites of A. alternata HSTs, and four cellular components, plasma membrane, mitochondrion, chloroplast and a metabolically important enzyme, have been identified as the primary sites of each HST action, leading to elucidation of the molecular mechanisms of HST sensitivity in host plants. Studies of the molecular genetics of HST production have identified supernumerary chromosomes encoding HST gene clusters and have provided new insights into the evolution of A. alternata pathotypes.

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Section: Acr-toxinmentioning

confidence: 99%

Host-selective toxins produced by the plant pathogenic fungusAlternaria alternata

et al. 2013

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“…The IBS* site is required as an acceptor site for transposition of the intron. A reverse transcriptase involved in this process is encoded by the pl‐intron 23. The outcome of these rather complex molecular processes is the duplication of intron sequences in the mtDNA.…”

Section: Age‐related Mtdna Instabilitiesmentioning

confidence: 99%

Mitochondrial Oxidative Stress and Aging in the Filamentous Fungus Podospora anserina

Osiewacz¹,

Borghouts²

2000

Annals of the New York Academy of Sciences

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In the filamentous fungus Podospora anserina, mitochondrial oxidative stress is a major contributor to aging. Reactive oxygen species (ROS) generated as a result of electron leakage during respiration lead to damage of components of the electron transport chain. In aging wild‐type cultures, damaged proteins cannot be replaced because the mitochondrial genes encoding some of the corresponding subunits gradually become deleted from the mitochondrial DNA (mtDNA). Consequently, these defects result in an increased generation of reactive oxygen species and respiration deficits leading to cell death. Analyses of wild‐type strains and of different long‐lived mutants of P. anserina provide strong evidence that molecular mechanisms controlling aging processes in this fungus are complex and act at different levels. A basic mechanism (e.g., damage by ROS) appears to be overlaid by prominent instabilities of the mtDNA.

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“…As with group I introns, group II IEPs facilitate in vivo intron splicing and intron mobility [94]. A well-characterized IEP is RT which was shown by an in vitro assay to have RNA-directed DNA polymerase activity with a sensitivity to RT inhibitors [95]. Later, experiments with yeast demonstrated the transposition of an mtDNA intron by a target DNA-primed reverse transcription [96].…”

Section: Rna-binding Proteins Are Involved In Chloroplast Splicingmentioning

confidence: 99%

Function of chloroplast RNA-binding proteins

Jacobs

Kück

2010

Cell. Mol. Life Sci.

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Chloroplasts are eukaryotic organelles which represent evolutionary chimera with proteins that have been derived from either a prokaryotic endosymbiont or a eukaryotic host. Chloroplast gene expression starts with transcription of RNA and is followed by multiple post-transcriptional processes which are mediated mainly by an as yet unknown number of RNA-binding proteins. Here, we review the literature to date on the structure and function of these chloroplast RNA-binding proteins. For example, the functional protein domains involved in RNA binding, such as the RNA-recognition motifs, the chloroplast RNA-splicing and ribosome maturation domains, and the pentatricopeptide-repeat motifs, are summarized. We also describe biochemical and forward genetic approaches that led to the identification of proteins modifying RNA stability or carrying out RNA splicing or editing. Such data will greatly contribute to a better understanding of the biogenesis of a unique organelle found in all photosynthetic organisms.

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Reverse transcriptase activity of an intron encoded polypeptide.

Cited by 48 publications

References 72 publications

Host-selective toxins produced by the plant pathogenic fungusAlternaria alternata

Host-selective toxins produced by the plant pathogenic fungusAlternaria alternata

Mitochondrial Oxidative Stress and Aging in the Filamentous Fungus Podospora anserina

Function of chloroplast RNA-binding proteins

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