Proteomics

Dataset Information

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Label-free shotgun proteomics of Triton X-100 insoluble fractions of Lon and FtsH conditional mutants of Mycoplasma pneumoniae under depleting and inducing conditions


ABSTRACT: Using Mycoplasma pneumoniae as a model organism, we conditionally depleted the two essential ATP-dependent proteases (Lon and FtsH) of this bacterium, by engineering strains carrying a Lon and/or FtsH inducible expression locus. An integrative comparative study combining label-free shotgun proteomics and RNA-seq allowed us to decipher the global cellular response to Lon and FtsH depletion and to define protease substrates in this genome-reduced organism. This particular dataset corresponds to the analysis of the Triton X-100 insoluble fractions of Lon and FtsH mutants grown under inducing and depleting conditions. The dataset for the whole cell lysate is available under the identifier PXD016343.

INSTRUMENT(S): LTQ Orbitrap Velos

ORGANISM(S): Mycoplasma Pneumoniae (strain Atcc 29342 / M129)

SUBMITTER: Marc Weber  

LAB HEAD: Luis Serrano

PROVIDER: PXD021506 | Pride | 2020-11-24

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
2020MM006_RABU_001_02_1ug.msf Msf
2020MM006_RABU_001_02_1ug.raw Raw
2020MM006_RABU_002_01_1ug.raw Raw
2020MM006_RABU_003_01_1ug.raw Raw
2020MM006_RABU_004_01_1ug.raw Raw
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Publications

Protein quality control and regulated proteolysis in the genome-reduced organism Mycoplasma pneumoniae.

Burgos Raul R   Weber Marc M   Martinez Sira S   Lluch-Senar Maria M   Serrano Luis L  

Molecular systems biology 20201201 12


Protein degradation is a crucial cellular process in all-living systems. Here, using Mycoplasma pneumoniae as a model organism, we defined the minimal protein degradation machinery required to maintain proteome homeostasis. Then, we conditionally depleted the two essential ATP-dependent proteases. Whereas depletion of Lon results in increased protein aggregation and decreased heat tolerance, FtsH depletion induces cell membrane damage, suggesting a role in quality control of membrane proteins. A  ...[more]

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