The structure and function of the gram-positive bacterial RNA degradosome
Open accessAbstract
The RNA degradosome is a highly structured protein complex responsible for bulk RNA decay in bacteria. The main components of the complex, ribonucleases, an RNA helicase, and glycolytic enzymes are well conserved in bacteria. Some components of the degradosome are essential for growth and the disruption of degradosome formation causes slower growth, indicating that this complex is required for proper cellular function. The study of the E. coli degradosome has been performed extensively for the last several decades and has revealed detailed information on its structure and function. On the contrary, the Gram-positive bacterial degradosome, which contains ribonucleases different from the E. coli one, has been studied only recently. Studies on the Gram-positive degradosome revealed that its major component RNase Y was necessary for the full virulence of medically important Gram-positive bacterial pathogens, suggesting that it could be a target of antimicrobial therapy. This review describes the structures and function of Gram-positive bacterial RNA degradosomes, especially those of a Gram-positive model organism Bacillus subtilis, and two important Gram-positive pathogens, Staphylococcus aureus and Streptococcus pyogenes.
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The degradosome is a complex consisting of a membrane-bound endoribonuclease scaffold (RNase Y), two metabolic enzymes (enolase and phosphofructokinase), an RNA helicase, a 3′ to 5′ exoribonuclease (RNase R or a putative exoribonuclease), and two 5′ to 3′ exoribonucleases (RNases J1 and J2).
“The degradosome is a complex that consists of a membrane-bound endoribonuclease scaffold (RNase Y), two metabolic enzymes (enolase and phosphofructokinase), an RNA helicase, a 3′ to 5′ exoribonuclease (RNase R or a putative exoribonuclease), and two 5′ to 3′ exoribonucleases (RNases J1 and J2) (Cho, 2017).”
From Fundamental behaviors emerge from simulations of a living minimal cell (2022) · cites this paper as Cho, 2017
Figure 2 and the B. subtilis RNA degradosome section identify RNase Y, enolase, phosphofructokinase, a DEAD-box helicase, and RNases J1 and J2 as components. But they identify PNPase—not RNase R or a putative exoribonuclease—as the degradosome’s 3′–5′ exoribonuclease; the S. aureus section also lists PNPase. (LLM, conf=0.90)
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“…is a complex that consists of a membranebound endoribonuclease scaffold (RNase Y), two metabolic enzymes (enolase and phosphofructokinase), an RNA helicase, a 3′ to 5′ exoribonuclease (RNase R or a putative exoribonuclease), and two 5′ to 3′ exoribonucleases (RNases J1 and J2) (Cho, 2017).”
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Function analysis of RNase E in the filamentous cyanobacterium Anabaena sp. PCC 7120
Yan, H., Cheng, Y., Wang, L., & Chen, W. (2020) · Research in Microbiology · doi:10.1016/j.resmic.2020.06.001 · Cited by 2 · see citing works
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Deciphering the function of Com_YlbF domain-containing proteins in Staphylococcus aureus
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Trans-acting regulators of ribonuclease activity
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The GT1 domain of RNase J ensures RNA quality control through dsRNA binding in Arabidopsis plastids
Baudry, K., Skiada, S., Burstein, C., Liveanu, V., Liehrmann, A., Ceminsky, M., Kleifeld, O., Delannoy, É., Launay‐Avon, A., Castandet, B., et al. (2026) · Nucleic Acids Research · doi:10.1093/nar/gkag033
- Authors
- Cho, K. H.
- Affiliations
- Indiana State University (US)
- Corresponding author
- Cho, Kyu Hong
- ORCID
- Cho, Kyu Hong
- Venue
- Frontiers in Microbiology
- Publisher
- Frontiers Media SA
- Published
- 2017-02-03
- Volume
- 8
- Pages
- 154-154
- ISSN
- 1664-302X (ISSN-L)
- PMC
- PMC5289998
- OpenAlex
- W2585190114
- Cited by
- 48
- References
- 58
- Citations by year
- 2026: 4 · 2025: 4 · 2024: 1 · 2023: 2 · 2022: 7 · 2021: 6 · 2020: 11 · 2019: 4 · 2018: 5 · 2017: 4
- FWCI
- 0.85
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- cc-by
- Locations
- Frontiers in Microbiology (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health (7R15 GM101603-02)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA Research and Splicing
- Keywords
- RNA degradosome, Gram-positive bacteria, RNase Y, ribonuclease, RNA helicase, glycolytic enzymes, Bacillus subtilis, Staphylococcus aureus, Streptococcus pyogenes, bacterial virulence, antimicrobial drug targets, protein complex structure
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