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Ribozymes

Ribozymes

The term ribozyme is used for RNA that can act as an enzyme. Ribozymes are mainly found in selected viruses, bacteria, plant organelles, and lower eukaryotes. Ribozymes were first discovered in 1982 when Tom Cech’s laboratory observed Group I introns acting as enzymes. This was shortly followed by the discovery of another ribozyme, Ribonulcease P, by Sid Altman’s laboratory. Both Cech and Altman received the Nobel Prize in chemistry in 1989 for their work on ribozymes.
Ribozymes can...

Ribozymes

Ribozymes

Eukaryotic RNA Polymerases

Eukaryotic RNA Polymerases

RNA Polymerase (RNAP) is conserved in all animals, with bacterial, archaeal, and eukaryotic RNAPs sharing significant sequence, structural, and functional similarities. Among the three eukaryotic RNAPs, RNA Polymerase II is most similar to bacterial RNAP in terms of both structural organization and folding topologies of the enzyme subunits. However, these similarities are not reflected in their mechanism of action.
All three eukaryotic RNAPs require specific transcription factors, of which the...

Eukaryotic RNA Polymerases

Eukaryotic RNA Polymerases

Bacterial RNA Polymerase

Bacterial RNA Polymerase

Unlike eukaryotes, bacteria use a single RNA Polymerase (RNAP) to transcribe all genes. The different subunits of bacterial RNAPhave distinct functions. The multisubunit structure of the bacterial RNAP helps the enzyme to maintain catalytic function, facilitate assembly, interact with DNA and RNA, and self-regulate its activity.
In most genes, the transcription site is a single base present upstream of the coding sequence. Though RNAP is a catalytically efficient enzyme, it does not recognize...

Bacterial RNA Polymerase

Bacterial RNA Polymerase

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Updated: Jan 10, 2026

A Fluorescence-based Exonuclease Assay to Characterize DmWRNexo, Orthologue of Human Progeroid WRN Exonuclease, and Its Application to Other Nucleases

A Fluorescence-based Exonuclease Assay to Characterize DmWRNexo, Orthologue of Human Progeroid WRN Exonuclease, and Its Application to Other Nucleases

Published on: December 23, 2013

Ribonuclease RNase Z is an evolutionarily conserved deAMPylase.

Meghomukta Mukherjee¹, Alex Pon¹, Timea Goldberg¹

¹Department of Physiology, University of Texas Southwestern Medical Center, Dallas, TX 75390.

Proceedings of the National Academy of Sciences of the United States of America

|November 20, 2025

Summary

This summary is machine-generated.

Researchers discovered that RNase Z removes adenosine monophosphate (AMP) from proteins, identifying it as a key enzyme in reversible protein AMPylation. This finding reveals a new role for RNase Z beyond its known function in tRNA processing.

Keywords:

AMPylation Endonuclease RNase BN adenylylation selenoprotein O

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Area of Science:

Biochemistry
Molecular Biology
Cellular Metabolism

Background:

Protein AMPylation is a conserved posttranslational modification where adenosine monophosphate (AMP) attaches to proteins.
Mitochondrial AMPylase, Selenoprotein O (SelO), regulates metabolism and oxidative stress via protein AMPylation.
The enzyme responsible for removing AMP from modified proteins was previously unknown.

Purpose of the Study:

To identify the enzyme that catalyzes deAMPylation of AMPylated protein substrates.
To elucidate the role of this enzyme in the reversible AMPylation pathway.
To understand the broader biological significance of RNase Z.

Main Methods:

Biochemical assays to test deAMPylation activity.
Enzyme kinetics studies.
In vitro and in vivo functional assays.

Main Results:

Ribonuclease Z (RNase Z) was identified as the enzyme responsible for deAMPylation.
RNase Z is both necessary and sufficient to remove AMP from AMPylated substrates.
This establishes RNase Z as a moonlighting enzyme with a novel function beyond tRNA processing.

Conclusions:

RNase Z catalyzes deAMPylation, revealing its role in reversible protein AMPylation.
The discovery highlights the importance of AMPylation as a regulatory mechanism, similar to phosphorylation.
RNase Z possesses a previously unrecognized biological function, expanding its known significance.