Feb 15, 2023 · RNA ligases play vital roles in sealing RNA strands during intron-containing tRNA splicing 1, tRNA repair 2, mRNA splicing in the unfolded-protein response (UPR) 3, RNA recombination 4, as...

The RNA ligase catalyzes the formation of 3′ → 5′ phosphodiester bonds between 3′-OH and 5′-P groups of RNA molecules. This reaction is coupled to the pyrophosphorolysis of ATP to AMP.

T4 RNA Ligase 1 catalyzes the ligation of a 5' phosphoryl-terminated nucleic acid donor to a 3' hydroxyl-terminated nucleic acid acceptor through the formation of a 3' - 5' phosphodiester bond with hydrolysis of ATP to AMP and PPi.

Feb 27, 2004 · In the current issue of Structure, Ho and coworkers report the crystal structure and mechanism of a T4 RNA ligase. These studies provide valuable insights on the mechanism and origin of RNA and DNA ligases, and RNA capping enzymes.

RNA repair pathways rely on RNA ligases to maintain or manipulate RNA structure in response to biologically purposeful RNA cleavage events. The goal of this project is to illuminate the mechanisms and structures of enzymes that repair broken RNA ends.

RNA ligation is a process that can be achieved with various intermediaries such as self-catalysing RNAs, 5′–3′ and 3′–5′ RNA ligases. While several types of RNA ligation mechanisms occur in human, RtcB is the only 3′–5′ RNA ligase identified in human cells to date.

Mar 16, 2024 · RNA ligases are found in all domains of life. They catalyze the ligation of RNA molecules via formation of phosphodiester bonds during different RNA processing and repair mechanisms. Among...

This unit describes specific reaction conditions, as well as applications such as radioactive labeling of the 3' termini of RNA, circularizing oligodeoxyribonucleotides and oligoribonucleotides, ligating oligomers and nicks, creating hybrid and chimeric …

We report the 1.9 A crystal structure of the ligase domain with AMP bound at the active site, which reveals a shared fold, catalytic mechanism, and evolutionary history for RNA ligases, DNA ligases, and mRNA capping enzymes.

We report the 1.9 Å crystal structure of the ligase domain with AMP bound at the active site, which reveals a shared fold, catalytic mechanism, and evolutionary history for RNA ligases, DNA ligases, and mRNA capping enzymes.