Dataset Information


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

ABSTRACT: 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. An integrative comparative study combining shotgun proteomics and RNA-seq revealed 62 and 34 candidate substrates, respectively. Cellular localization of substrates and epistasis studies supports separate functions for Lon and FtsH. Protein half-life measurements also suggest a role for Lon-modulated protein decay. Lon plays a key role in protein quality control, degrading misfolded proteins and those not assembled into functional complexes. We propose that regulating complex assembly and degradation of isolated proteins is a mechanism that coordinates important cellular processes like cell division. Finally, by considering the entire set of proteases and chaperones, we provide a fully integrated view of how a minimal cell regulates protein folding and degradation.


PROVIDER: S-EPMC7737663 | BioStudies | 2020-01-01

REPOSITORIES: biostudies

Similar Datasets

2020-11-10 | E-MTAB-8537 | ArrayExpress
2020-11-10 | E-MTAB-8537 | BioStudies
2019-01-01 | S-EPMC6567685 | BioStudies
2020-11-24 | PXD016343 | Pride
2018-01-01 | S-EPMC5892824 | BioStudies
1000-01-01 | S-EPMC2893105 | BioStudies
2018-01-01 | S-EPMC6098112 | BioStudies
2020-11-24 | PXD021506 | Pride
2010-01-01 | S-EPMC2906341 | BioStudies
| S-EPMC3273809 | BioStudies