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Proteome wide measurements of protein half-lives in Mycoplasma pneumoniae

ABSTRACT: We obtained proteome wide measurements of protein half-lives in M. pneumoniae by performing pulse-chase experiments following SILAC methods. We estimated degradation rates of individual proteins by measuring the increase in light protein compared to heavy protein labeling along the growth curve.

INSTRUMENT(S): LTQ Orbitrap Velos

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

TISSUE(S): Cell Culture

SUBMITTER: Marc Weber

LAB HEAD: Luis Serrano

PROVIDER: PXD016386 | Pride | 2020-11-24

REPOSITORIES: Pride

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			Action	DRS
	160727_S_SMLS_01_01_fasp_2ug-01.msf	Msf
	160727_S_SMLS_01_01_fasp_2ug.raw	Raw
	160727_S_SMLS_02_01_fasp_2ug.raw	Raw
	160727_S_SMLS_03_01_fasp_2ug.raw	Raw
	160727_S_SMLS_04_01_fasp_2ug.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]

PMID: 33320415

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Label-free shotgun proteomics of Lon and FtsH conditional mutants of Mycoplasma pneumoniae under depleting and inducing conditions

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Label-free shotgun proteomics of M. hyopneumoniae and M. feriruminatoris

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