Evolutionary changes in key enzyme may help bacteria make proteins faster
Researchers have identified evolutionary changes in the enzyme IleRS that allow bacteria to synthesize proteins more efficiently. By remodeling the C-terminal region, these organisms have optimized the speed of aminoacylation, a critical step in protein production.
Why it matters
Understanding how bacteria evolve to optimize protein synthesis provides insights into fundamental biological processes and potential targets for future antimicrobial therapies.
edited by Sadie Harley , reviewed by Robert Egan
This article has been reviewed according to Science X's editorial process and policies . Editors have highlighted the following attributes while ensuring the content's credibility:
Add to Preferred Sources Researchers traced how evolutionary remodeling of IleRS altered its interactions with tRNA and its enzyme activity, revealing structural changes consistent with selection for faster aminoacylation in prokaryotes. Credit: Institute of Science Tokyo, Japan Evolutionary changes in a key protein synthesis enzyme, isoleucyl-tRNA synthetase (IleRS), may help bacteria fine-tune how quickly proteins are made, report researchers from Institute of Science Tokyo, Japan; the University of Zagreb Faculty of Science, Croatia; and ETH Zürich, Switzerland.
Researchers traced the enzyme's evolutionary history and identified three distinct IleRS clades. Their findings show that C-terminal remodeling, including repeated loss of a structural region called "INS," may have helped refine enzyme activity and reaction speed.
Also covering this story
One other newsroom covered this event. We read that version too.
Get smarter about the news
Sign up free for a feed built around what you actually care about, Dive Deeper research on any story, and the full text of every article.
Create free accountAlready have an account? Sign in