🔽 (the first) ribosomal E-site targeting antibacterial; producer avoids self-toxicity by rRNA methylation. #Ribosome #AMR
Nature research paper: A natural depsipeptide antibiotic binds the E-site of the bacterial ribosome
go.nature.com/3RMNwPW
Researchers say they have used a precise genome-editing technique called base editing to alter the genome of human embryos for the first time, an announcement that prompted both excitement and dismay.
go.nature.com/3RUBKD6
Frances Yap
The latest from the lab. Manikomycin, a new cyclic depsipeptide antibiotic from an 'old' source, the oxytetracycline producer Streptomyces rimosus. Still lots to be learned from this genus! Manikomycin blocks the E-site of the bacterial ribosome. A first.
links.springernature.com/f/a/Q0JMeeZK...
Improved fractionation strategies can identify antibiotics with previously unseen scaffolds and mechanisms, exemplified by manikomycin from Streptomyces rimosus, which acts by targeting the E-site of the bacterial large ribosomal subunit.
go.nature.com
The lead scientist on the use of ‘base editing’ in very early embryos say that the technique is far from ready for the clinic, but critics worry that the work will spur a rush to commercialization.
Improved fractionation strategies can identify antibiotics with previously unseen scaffolds and mechanisms, exemplified by manikomycin from Streptomyces rimosus, which acts by targeting the E-site of ...
Diverse mechanisms of translation arrest by a Clostridia ribosome stalling peptide CliM - pubmed.ncbi.nlm.nih.gov/42151144/
Ribosome arrest peptides undergo programmed translational stalling in response to changes in the cellular environment to feedback-regulate gene expression. CliM, an arrest peptide in Clostridia, is en...
New paper in @natcomms.nature.com! We show how the Clostridia peptide CliM acts as a molecular handbrake to monitor YidC activity.
Cryo-EM & MD show it stalls the ribosome using diverse mechanisms until membrane insertion releases it.
Paper: www.nature.com/articles/s41...
Wiep Klaas Smits (ExpBac/CMAT)
🚨 New in @natcomms.nature.com 🚨
Excited to share our paper on how proline-rich antimicrobial peptides interact with the bacterial ribosome.
Using cryo-EM, we found that tiny sequence changes cause these peptides to "flip" orientation in the exit tunnel! 🔄🧫
Read: www.nature.com/articles/s41...
www.nature.com/articles/s41...
www.nature.com
CliM is a ribosome arrest peptide in Clostridia. Here, the authors show that CliM adopts helices and extensively interacts with the ribosome. The penultimate residue sterically blocks A-site accommoda...
In this work authors show how minimal mutations in proline-rich antimicrobial peptides can flip their orientation in the ribosome exit tunnel, switching their mechanism from stalling translation termi...
In this work authors show how minimal mutations in proline-rich antimicrobial peptides can flip their orientation in the ribosome exit tunnel, switching their mechanism from stalling translation termi...
🧪🦠Streptomyces rimosus
"Das Antibiotikum mit dem Namen Manikomycin wirkt gegen multiresistente Bakterien und könnte langfristig zur Entwicklung neuer Behandlungsoptionen beitragen"
www.welt.de/gesundheit/a...
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www.nature.com/articles/s41...
www.welt.de
Ausgerechnet ein lange erforschter Mikroorganismus liefert einen bislang unbekannten Wirkstoff gegen multiresistente Keime. Manikomycin ist noch weit von der Klinik entfernt – zeigt aber, wo die Antib...
Improved fractionation strategies can identify antibiotics with previously unseen scaffolds and mechanisms, exemplified by manikomycin from Streptomyces rimosus, which acts by targeting the E-site of ...
