Cited by 210RNA and protein synthesis mechanismsBacterial Genetics and BiotechnologyHeat shock proteins research

The bacterial translation stress response.

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Starosta, Agata L., Lassak, Jürgen, Jung, Kirsten, Wilson, Daniel N.·2014·FEMS Microbiology Reviews

Abstract

Throughout their life, bacteria need to sense and respond to environmental stress. Thus, such stress responses can require dramatic cellular reprogramming, both at the transcriptional as well as the translational level. This review focuses on the protein factors that interact with the bacterial translational apparatus to respond to and cope with different types of environmental stress. For example, the stringent factor RelA interacts with the ribosome to generate ppGpp under nutrient deprivation, whereas a variety of factors have been identified that bind to the ribosome under unfavorable growth conditions to shut-down (RelE, pY, RMF, HPF and EttA) or re-program (MazF, EF4 and BipA) translation. Additional factors have been identified that rescue ribosomes stalled due to stress-induced mRNA truncation (tmRNA, ArfA, ArfB), translation of unfavorable protein sequences (EF-P), heat shock-induced subunit dissociation (Hsp15), or antibiotic inhibition (TetM, FusB). Understanding the mechanism of how the bacterial cell responds to stress will not only provide fundamental insight into translation regulation, but will also be an important step to identifying new targets for the development of novel antimicrobial agents.

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Crossref · 10.1111/1574-6976.12083

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  • The ribosomal protein genes in the spc operon are significantly down-regulated during stationary phase or when cells encounter stress conditions.

    “These genes are significantly down-regulated during stationary phase or when cells encounter stress conditions (Coenye and Vandamme, 2005; Ikegami et al., 2005; Starosta et al., 2014).”

    From The Dynamic SecYEG Translocon (2021) · cites this paper as Starosta et al., 2014

  • RelA primarily responds to stalled ribosomes upon amino acid starvation.

    “RelA primarily responds to stalled ribosomes upon amino acid starvation (Starosta et al., 2014; Steinchen et al., 2020), while SpoT activity increases upon fatty acid or carbon starvation (Battesti and Bouveret, 2009; Figure 12).”

    From The Dynamic SecYEG Translocon (2021) · cites this paper as Starosta et al., 2014

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References 254 · Cited by 210

Authors
Starosta, A. L., Lassak, J., Jung, K., & Wilson, D. N.
Affiliations
Center for Integrated Protein Science Munich (DE)
Corresponding author
Wilson, Daniel N.
Venue
FEMS Microbiology Reviews
Published
2014-11
Volume
38
Issue
6
Pages
1172-1201
ISSN
  • 0168-6445 (ISSN-L)
  • 1574-6976
OpenAlex
W2147484502
Cited by
210
References
254
Citations by year
2026: 8 · 2025: 23 · 2024: 13 · 2023: 12 · 2022: 18 · 2021: 20 · 2020: 22 · 2019: 15 · 2018: 17 · 2017: 27 · 2016: 19 · 2015: 15 · 2014: 1
FWCI
1.95
Type
journal article
Language
en
Open access
Locations
  • FEMS Microbiology Reviews (publishedVersion)
  • PubMed (publishedVersion)
  • PubMed Central (acceptedVersion)
Funders
  • Deutsche Forschungsgemeinschaft (FOR1805, WI3285/4-1, Exc114-2)
  • National Institutes of Health (NIHR01GM095737)
  • EMBO (YIP)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
Keywords
stringent response, RelA, ppGpp, RelE, RMF, HPF, MazF, Indonesian as a foreign language, tmRNA, ArfA, elongation factor P, tetM, ribosome-associated proteins, translational regulation, nutrient deprivation, antibiotic inhibition, antimicrobial drug targets
MeSH terms
Anti-Bacterial Agents, Bacteria, Protein Binding, Ribosomes, RNA, Messenger, Stress, Physiological, Gene Expression Regulation, Bacterial, Bacterial Physiological Phenomena

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