Work

Metastable Folding of Bacillus subtilis glmS Ribozyme Modulates Turnover by RNase J1

Year: 2025

Type: article

Abstract: Rapid turnover of glmS mRNA in Bacillus subtilis by 5′-3’ exoribonuclease RNase J is essential for feedback regulation of glucosamine-6-phosphate (GlcN6P) synthase expression, upon self-cleavage of a GlcN6P-activated ribozyme in the glmS 5′ UTR. We used biochemical assays and single molecule fluorescence microscopy to show that initiation of RNase J decay is inefficient and requires approximately 15 5′ unpaired nucleotides to form a processive exonuclease complex that is insensitive to downstream RNA structure. When stably folded, the cleaved glmS ribozyme blocks RNase J initiation. However, co-transcriptional ribozyme cleavage and physiological Mg 2+ levels increase decay by weakening the ribozyme structure. At 22 ˚C, the processive velocity of RNase J, 23 ± 8 nt/s, is equal or faster than transcription, indicating that RNase J has the potential to catch elongating polymerases. The results show how the folding stability of 5′ mRNA structure contributes to RNase J recognition and the control of mRNA half-life.

Source: Journal of Molecular Biology

DOI: 10.1016/j.jmb.2025.169612

Authors: Yuan Lou, Sarah A. Woodson

Institution: Johns Hopkins University

Language: English

Topic: RNA and protein synthesis mechanisms

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: hybrid

Estimated APC paid: $4,730

Funders: National Institutes of Health, National Institute of General Medical Sciences