AI Article Synopsis
- MthRnl is an enzyme that connects RNA strands by forming bonds between their ends and can convert RNA with a 3'-phosphate end into a different structure.
- The enzyme also removes adenosine from the end of RNA, a process requiring metal ions and specific molecular conditions.
- These properties indicate that MthRnl may play a role in managing certain types of RNA, influencing how they function and interact in biological processes.
Article Abstract
Methanothermobacter thermoautotrophicus RNA ligase (MthRnl) catalyzes formation of phosphodiester bonds between the 5'-phosphate and 3'-hydroxyl termini of single-stranded RNAs. It can also react with RNA with a 3'-phosphate end to generate a 2',3'-cyclic phosphate. Here, we show that MthRnl can additionally remove adenosine from the 3'-terminus of the RNA to produce 3'-deadenylated RNA, RNA(3'-rA). This 3'-deadenylation activity is metal-dependent and requires a 2'-hydroxyl at both the terminal adenosine and the penultimate nucleoside. Residues that contact the ATP/AMP in the MthRnl crystal structures are essential for the 3'-deadenylation activity, suggesting that 3'-adenosine may occupy the ATP-binding pocket. The 3'-end of cleaved RNA(3'-rA) consists of 2',3'-cyclic phosphate which protects RNA(3'-rA) from ligation and further deadenylation. These findings suggest that ATP-dependent RNA ligase may act on a specific set of 3'-adenylated RNAs to regulate their processing and downstream biological events.
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5599603 | PMC |
| http://dx.doi.org/10.1038/s41598-017-11693-0 | DOI Listing |
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