MIT News breed · Science

New Enzyme Discovery Aids Understanding of Bacterial Adaptation

Scientists identified aminovaleramididine synthetase (AvaS), a novel enzyme modifying RNA, offering insights into bacterial adaptation and potential antimicrobial resistance strategies.

Led by SMART AMR, an international team discovered AvaS, the first PLP-dependent enzyme linked to RNA modification. This finding advances understanding of bacterial adaptation and potential antimicrobial targets.

Bacteria use tRNA modifications to control protein production under stress. AvaS creates aminovaleramide cytidine (ava2C) in Pseudomonas aeruginosa, a bacterium causing serious infections.

The research, published in Nature Chemical Biology, identified AvaS after screening bacterial mutants. Ava2C was also found in Acinetobacter baumannii, Vibrio cholerae, and the plant Arabidopsis thaliana.

AvaS uses PLP to convert lysidine (k2C) into ava2C, marking the first PLP-dependent enzyme linked to tRNA modification. This expands known enzyme functions beyond metabolism.

Ava2C alters genetic code reading, enabling faster protein production and adaptation to stress. This discovery classifies PLP-dependent enzymes as a new group of tRNA-modifying enzymes.

Future research will explore Ava2C's impact on bacterial stress responses and metabolism, and potential disruption methods. The findings also suggest broader implications for other organisms.

This work highlights the utility of SMART AMR's epitranscriptomics platform for discovering novel RNA-modifying enzymes and potential drug targets.

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