Proteomics

Dataset Information

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Proteome of WT and CLPP-null Podospora Anserina

ABSTRACT: Mutations in the gene for the mitochondrial matrix protease CLPP can cause human Perrault syndrome, which is characterized by male and female infertility, progressive sensorineural deafness, ataxia and leukoencephalopathy. This gene encodes a peptidase that is conserved since bacteria and localizes to mitochondrial matrix in eukaryotes. To compare and validate mouse and human findings, the filamentous fungus Podospora anserina was cultured and protein extracts were analyzed.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Podospora Anserina

TISSUE(S): Cell Culture

SUBMITTER: Jana Key  

LAB HEAD: Prof. Georg Auburger

PROVIDER: PXD048640 | Pride | 2024-06-22

REPOSITORIES: Pride

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Dataset's files

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Action DRS
Data_analysis.xlsx Xlsx
Kurzgele.tif Other
P18_078_Podospora_Sample02_01.raw Raw
P18_078_Podospora_Sample02_02.raw Raw
P18_078_Podospora_Sample02_03.raw Raw
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Publications

CLPP-Null Eukaryotes with Excess Heme Biosynthesis Show Reduced L-arginine Levels, Probably via CLPX-Mediated OAT Activation.

Key Jana J   Gispert Suzana S   Kandi Arvind Reddy AR   Heinz Daniela D   Hamann Andrea A   Osiewacz Heinz D HD   Meierhofer David D   Auburger Georg G  

Biomolecules 20240219 2

The serine peptidase CLPP is conserved among bacteria, chloroplasts, and mitochondria. In humans and mice, its loss causes Perrault syndrome, which presents with growth deficits, infertility, deafness, and ataxia. In the filamentous fungus <i>Podospora anserina</i>, CLPP loss leads to longevity. CLPP substrates are selected by CLPX, an AAA+ unfoldase. CLPX is known to target delta-aminolevulinic acid synthase (ALAS) to promote pyridoxal phosphate (PLP) binding. CLPX may also influence cofactor a  ...[more]

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