Protein aggregates encode epigenetic memory of stressful encounters in individual Escherichia coli cells

Autor: Abram Aertsen, Antoine Adam, Julien Mortier, Sander K. Govers
Jazyk: angličtina
Rok vydání: 2018
Předmět:
0301 basic medicine
Life Sciences & Biomedicine - Other Topics
Protein Folding
Hot Temperature
Gene Expression
Protein aggregation
Epigenesis
Genetic
Single-cell analysis
Mutant protein
Genes
Reporter
Biology (General)
Heat-Shock Proteins
IN-VIVO
IBPB
General Neuroscience
Escherichia coli Proteins
Adaptation
Physiological
Cell biology
Anti-Bacterial Agents
FLUORESCENT PROTEINS
Streptomycin
Single-Cell Analysis
General Agricultural and Biological Sciences
Life Sciences & Biomedicine
Intracellular
EXPRESSION
Biochemistry & Molecular Biology
QH301-705.5
030106 microbiology
Green Fluorescent Proteins
Biology
HIGH-THROUGHPUT
TRANSCRIPTIONAL RESPONSE
General Biochemistry
Genetics and Molecular Biology
03 medical and health sciences
Protein Aggregates
Stress
Physiological
Escherichia coli
SEGREGATION
Epigenetics
Heat shock
Science & Technology
General Immunology and Microbiology
Robustness (evolution)
Hydrogen Peroxide
YEAST PRION
Luminescent Proteins
030104 developmental biology
Proteostasis
RECOMBINANT PROTEIN
SMALL HEAT-SHOCK
Zdroj: PLoS Biology, Vol 16, Iss 8, p e2003853 (2018)
ISSN: 1545-7885
1544-9173
Popis: Protein misfolding and aggregation are typically perceived as inevitable and detrimental processes tied to a stress- or age-associated decline in cellular proteostasis. A careful reassessment of this paradigm in the E. coli model bacterium revealed that the emergence of intracellular protein aggregates (PAs) was not related to cellular aging but closely linked to sublethal proteotoxic stresses such as exposure to heat, peroxide, and the antibiotic streptomycin. After removal of the proteotoxic stress and resumption of cellular proliferation, the polarly deposited PA was subjected to limited disaggregation and therefore became asymmetrically inherited for a large number of generations. Many generations after the original PA-inducing stress, the cells inheriting this ancestral PA displayed a significantly increased heat resistance compared to their isogenic, PA-free siblings. This PA-mediated inheritance of heat resistance could be reproduced with a conditionally expressed, intracellular PA consisting of an inert, aggregation-prone mutant protein, validating the role of PAs in increasing resistance and indicating that the resistance-conferring mechanism does not depend on the origin of the PA. Moreover, PAs were found to confer robustness to other proteotoxic stresses, as imposed by reactive oxygen species or streptomycin exposure, suggesting a broad protective effect. Our findings therefore reveal the potential of intracellular PAs to serve as long-term epigenetically inheritable and functional memory elements, physically referring to a previous cellular insult that occurred many generations ago and meanwhile improving robustness to a subsequent proteotoxic stress. The latter is presumably accomplished through the PA-mediated asymmetric inheritance of protein quality control components leading to their specific enrichment in PA-bearing cells. ispartof: PLOS BIOLOGY vol:16 issue:8 ispartof: location:United States status: published
Databáze: OpenAIRE
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