Neue Enzyme für ein altes Organell: Kryptische peroxisomale Lokalisationssignale
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Philipps-Universität Marburg
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Abstract
Peroxisomes are near-ubiquitous eukaryotic organelles with a general function in the β-
oxidation of fatty acids and hydrogen peroxide detoxification. Additionally peroxisomes
exhibit more specific metabolic function in different organisms including parts of the
reactions of the glyoxylate cycle in plants and fungi and the production of secondary
metabolites. A special type of peroxisomes has been identified in trypanosomes. In these
parasites the majority of glycolytic enzymes is localized in peroxisomes.
All types of peroxisomes are characterized by a unique protein import system. Peroxisomal
matrix proteins contain C-terminal or N-terminal PTS (peroxisomal targeting signal) motifs
(C-terminal: PTS1; N-Terminal: PTS2), which are recognized by soluble receptors mediating
the import of fully folded and even oligomeric proteins.
Studies on mRNA processing in the plant pathogenic fungus Ustilago maydis lead to the
unexpected discovery of isoforms of glycolytic enzymes harboring PTS1 motifs. These
isoforms result from alternative splicing and translational read-through, respectively. A
bioinformatic survey revealed the presence of such isoforms in many fungal species, although
the mechanisms giving rise to PTS1 motifs vary between species. Some glycolytic enzymes
were shown to possess low efficiency PTS1 motifs differing from the PTS1 consensus
sequence. These motifs might also lead to dual cytoplasmic and peroxisomal targeting similar
to the already described mechanisms.
More detailed analysis of peroxisomes in U. maydis established additional functions of these
organelles in sugar metabolism and pathogenic development beside their prominent role in
the breakdown of fatty acids. Moreover, it could be demonstrated that peroxisomes participate
in the production of glycolipids in U. maydis.
The data obtained here suggests novel metabolic functions for peroxisomes at least in fungi.
The identification of cryptic PTS1 motifs in glycolytic enzymes in fungi indicates that
peroxisomes of other organisms likely contain a variety of unexpected proteins.
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Dates
Created: 2013Issued: 2014-04-10Updated: 2014-04-10
Faculty
Fachbereich Biologie
Publisher
Philipps-Universität Marburg
Language
ger
Data types
DoctoralThesis
Keywords
peroxisomeTranslational readthroughalternative splicingStopcodonglycolysisdual localizationDuale Lokalisierung
DFG-subjects
Ustilago zeaePeroxisomGlykolyseSpleißenProteintransport
DDC-Numbers
570
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Freitag, Johannes (1049796675): Neue Enzyme für ein altes Organell: Kryptische peroxisomale Lokalisationssignale. : Philipps-Universität Marburg 2014-04-10. DOI: https://doi.org/10.17192/z2013.0477.
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This item has been published with the following license: In Copyright