ArticleScientific reports2013
Escherichia coli transcription termination factor NusA: heat-induced oligomerization and chaperone activity.
Article in Scientific reports, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed.
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- Early transcriptional changes of heavy metal resistance and multiple efflux genes in Xanthomonas campestris pv. campestris under copper and heavy metal ion stress.BMC microbiology · 2024Article
- Factors involved in heterologous expression of proteins in E. coli host.Archives of microbiology · 2023Review
- Structural basis of AlpA-dependent transcription antitermination.Nucleic acids research · 2022Article
- SHTXTHHly, an extracellular secretion platform for the preparation of bioactive peptides and proteins in Escherichia coli.Microbial cell factories · 2022Article
- Predictive approaches to guide the expression of recombinant vaccine targets in Escherichia coli: a case study presentation utilising Absynth Biologics Ltd. proprietary Clostridium difficile vaccine antigens.Applied microbiology and biotechnology · 2021Article
- Amikacin and bacteriophage treatment modulates outer membrane proteins composition in Proteus mirabilis biofilm.Scientific reports · 2021Article
- Emerging Adaptive Strategies Under Temperature Fluctuations in a Laboratory Evolution Experiment ofFrontiers in microbiology · 2021Article
- Structural basis of transcription-translation coupling.Science (New York, N.Y.) · 2020Article
- Understanding Stress Response to High-Arsenic Gold-Bearing Sulfide Concentrate in Extremely Metal-Resistant AcidophileMicroorganisms · 2020Article
- Complete genome of streamlined marine actinobacterium Pontimonas salivibrio strain CL-TW6BMC genomics · 2018Article
- Protein Composition ofFrontiers in microbiology · 2018Article
- Universal Stress Protein Exhibits a Redox-Dependent Chaperone Function in Arabidopsis and Enhances Plant Tolerance to Heat Shock and Oxidative Stress.Frontiers in plant science · 2015Article
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Authors and funding
8 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Escherichia coli NusA, an essential component of the RNA polymerase elongation complex, is involved in transcriptional elongation, termination, anti-termination, cold shock and stress-induced mutagenesis. In this study, we demonstrated that NusA can self-assemble into oligomers under heat shock conditions and that this property is largely determined by the C-terminal domain. In parallel with the self-assembly process, NusA also acquires chaperone activity. Furthermore, NusA overexpression results in the enhanced heat shock resistance of host cells, which may be due to the chaperone activity of NusA. Our results suggest that E. coli NusA can act as a protector to prevent protein aggregation under heat stress conditions in vitro and in the NusA-overexpressing strain. We propose a new hypothesis that NusA could serve as a molecular chaperone in addition to its functions as a transcription factor. However, it remains to be further investigated whether NusA has the same function under normal physiological conditions.
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