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Pupylation-independent substrate recruitment to proteasomal degradation in mycobacteria

ABSTRACT: Mycobacteria and other Actinobacteria possess proteasomal degradation pathways in addition to the common bacterial compartmentalizing protease systems. Proteasomal degradation supports survival of these bacteria in adverse environments and conditions. The mycobacterial proteasome interacts with multiple ring-shaped activators, including the bacterial proteasome activator (Bpa), which facilitates the energy-independent degradation of heat shock repressor HspR in the successful human pathogen M. tuberculosis. To explore if this observation can be corroborated in the soil bacterium M. smegmatis, we performed an enrichment study in a bpa knockout in M. smegmatis. We grew the wild type M. smegmatis strain and the bpa knockout strain in biological triplicates under standard conditions or under heat shock and analyzed proteins which increased in abundance by data-independent acquisition mass spectrometry.

INSTRUMENT(S): Orbitrap Eclipse

ORGANISM(S): Mycobacterium Smegmatis (strain Atcc 700084 / Mc(2)155)

TISSUE(S): Bone Marrow

SUBMITTER: Monika Pepelnjak

LAB HEAD: Eilika Weber-Ban

PROVIDER: PXD039021 | Pride | 2023-08-04

REPOSITORIES: pride

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			Action	DRS
	20221130_075608_210217_pmonika_C1_exp4_Report.tsv	Tabular
	210212_pmonika_C1_83.raw	Raw
	210212_pmonika_C1_84.raw	Raw
	210212_pmonika_C1_85.raw	Raw
	210212_pmonika_C1_86.raw	Raw

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Project description:Proctor2005 - Actions of chaperones and their role in ageing This model is described in the article: Modelling the actions of chaperones and their role in ageing. Proctor CJ, Soti C, Boys RJ, Gillespie CS, Shanley DP, Wilkinson DJ, Kirkwood TB. Mech. Ageing Dev. 2005 Jan; 126(1): 119-131 Abstract: Many molecular chaperones are also known as heat shock proteins because they are synthesised in increased amounts after brief exposure of cells to elevated temperatures. They have many cellular functions and are involved in the folding of nascent proteins, the re-folding of denatured proteins, the prevention of protein aggregation, and assisting the targeting of proteins for degradation by the proteasome and lysosomes. They also have a role in apoptosis and are involved in modulating signals for immune and inflammatory responses. Stress-induced transcription of heat shock proteins requires the activation of heat shock factor (HSF). Under normal conditions, HSF is bound to heat shock proteins resulting in feedback repression. During stress, cellular proteins undergo denaturation and sequester heat shock proteins bound to HSF, which is then able to become transcriptionally active. The induction of heat shock proteins is impaired with age and there is also a decline in chaperone function. Aberrant/damaged proteins accumulate with age and are implicated in several important age-related conditions (e.g. Alzheimer's disease, Parkinson's disease, and cataract). Therefore, the balance between damaged proteins and available free chaperones may be greatly disturbed during ageing. We have developed a mathematical model to describe the heat shock system. The aim of the model is two-fold: to explore the heat shock system and its implications in ageing; and to demonstrate how to build a model of a biological system using our simulation system (biology of ageing e-science integration and simulation (BASIS)). This model is hosted on BioModels Database and identified by: BIOMD0000000091. To cite BioModels Database, please use: BioModels Database: An enhanced, curated and annotated resource for published quantitative kinetic models. To the extent possible under law, all copyright and related or neighbouring rights to this encoded model have been dedicated to the public domain worldwide. Please refer to CC0 Public Domain Dedication for more information.

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Pupylation-independent substrate recruitment to proteasomal degradation in mycobacteria

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