Draft:Balon (protein)
| Submission declined on 24 July 2024 by Mgp28 (talk). The proposed article does not have sufficient content to require an article of its own, but it could be merged into the existing article at Hibernation factor. Since anyone can edit Wikipedia, you are welcome to add that information yourself. Thank you.
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Comment: I liked this article a lot but I cannot currently find enough sources to convince me that it meets Wikipedia's notability criteria. Given the protein is only recently discovered, I suspect it could meet the criteria in the future. In the meantime, I suggest you merge this text into Hibernation factor (which you also created), then split it off once there is enough coverage in reliable sources. Mgp28 (talk) 15:37, 24 July 2024 (UTC)
 | An editor has marked this as a promising draft and requests that, should it go unedited for six months, G13 deletion be postponed, either by making a dummy/minor edit to the page, or by improving and submitting it for review. Last edited by Mrfoogles (talk | contribs) 6 days ago. (Update) |  |
| Balon | |
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_in_complex_with_Mycobacterium_smegmatis_70S_ribosome.png) A rendering of Msmeg1130 (Balon analogue) in a complex with the Mycobacterium smegmatis ribosome. Balon in tan in the center. | |
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Balon is a hibernation factor protein found in the cold-adapted bacterium Psychrobacter urativorans.[1] "Balon" means "ball" in Spanish. The name was chosen to match Pelota, a possible distant homologue whose name is also a Spanish word for "ball."[1] Balon binds to the ribosome in order to halt the production of proteins, which can account for more than 50% of a cell's energy usage, when the cell enters a dormant state.[2] Unlike previously discovered hibernation factors, Balon can bind to the ribosome while protein production is in process.[2] This is important for rapid response to stress because in some cells, protein production can take up to 20 minutes to complete.[3] Balon does this by rather than physically blocking the A site of the ribosome, as other hibernation factors do, binding near to but not across the channel, allowing it to attach to the ribosome independent of whether protein production is taking place.[2] Balon was discovered accidentally by a researcher who unintentionally left a sample of P. urativorans in an ice bucket for too long, cold-shocking it, through subsequent cryo-EM scans of the organism's ribosomes.[2]
Relatives of Balon have been found which bind to ribosome A-sites in Mycobacterium tuberculosis, which causes tuberculosis, and Thermus thermophilus, which lives in thermal vents, suggesting that it has similarly acting homologues in other species.[2] Genetic relatives of Balon have been found in 20% of bacterial genomes catalogued in public databases, but were not found in Escherichia coli and Staphylococcus aureus, which are commonly used in studies of cellular dormancy.[2]
References
[edit]- ^ a b Helena-Bueno, Karla; Rybak, Mariia Yu; Ekemezie, Chinenye L.; Sullivan, Rudi; Brown, Charlotte R.; Dingwall, Charlotte; Baslé, Arnaud; Schneider, Claudia; Connolly, James P. R.; Blaza, James N.; Csörgő, Bálint; Moynihan, Patrick J.; Gagnon, Matthieu G.; Hill, Chris H.; Melnikov, Sergey V. (14 February 2024). "A new family of bacterial ribosome hibernation factors". Nature. 626 (8001): 1125–1132. Bibcode:2024Natur.626.1125H. doi:10.1038/s41586-024-07041-8. ISSN 1476-4687. PMC 10901736. PMID 38355796.
- ^ a b c d e f Samorodnitsky, Dan (2024-06-05). "Most Life on Earth is Dormant, After Pulling an 'Emergency Brake'". Quanta Magazine. Retrieved 2024-06-09.
- ^ York, University of. "York research delivers new understanding of cells' survival ability". University of York. Retrieved 2024-06-09.