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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.
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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...

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Ribosomal RNA Synthesis

Ribosomal RNA Synthesis

Ribosome synthesis is a highly complex and coordinated process involving more than 200 assembly factors. The synthesis and processing of ribosomal components occurs not only in the nucleolus but also in the nucleoplasm and the cytoplasm of eukaryotic cells.
Ribosome biogenesis begins with the synthesis of 5S and 45S pre-rRNAs by distinct RNA polymerases. The primary transcripts are extensively processed and modified before they are bound and folded by ribosomal proteins and assembly factors,...

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Updated: Mar 9, 2026

RIBO-seq in Bacteria: a Sample Collection and Library Preparation Protocol for NGS Sequencing

RIBO-seq in Bacteria: a Sample Collection and Library Preparation Protocol for NGS Sequencing

Published on: August 7, 2021

Ribonuclease E: Chopping Knife and Sculpting Tool.

Joel G Belasco¹

¹Kimmel Center for Biology and Medicine at the Skirball Institute and Department of Microbiology, New York University School of Medicine, 540 First Avenue, New York, NY 10016, USA.

|January 7, 2017

Summary

The bacterial enzyme RNase E acts as both a degradative enzyme and an RNA maturase. This dual function is crucial for shaping the transcriptome of bacterial pathogens.

Keywords:

RNA decay RNA degradation RNA maturation RNA processing RNA stability RNA-seq RNase E Salmonella endoribonuclease sRNA

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Area of Science:

Bacterial molecular biology
RNA processing and degradation
Transcriptome dynamics

Background:

The bacterial enzyme RNase E plays a critical role in RNA processing.
Its known function involves degrading RNA molecules.
The broader impact of RNase E on the bacterial transcriptome is not fully understood.

Purpose of the Study:

To investigate the multifaceted role of RNase E in bacterial pathogens.
To elucidate how RNase E functions as both a degradative enzyme and an RNA maturase.
To understand the contribution of RNase E to shaping the bacterial transcriptome.

Main Methods:

Biochemical assays to assess RNase E enzymatic activity.
RNA sequencing (RNA-Seq) to analyze transcriptome-wide changes.
Mutational analysis of RNase E to determine functional domains.

Main Results:

RNase E exhibits both RNA degradation and RNA maturation activities.
These dual functions significantly influence the stability and processing of various RNA species.
Specific RNA targets of RNase E were identified, demonstrating its role in transcriptome architecture.

Conclusions:

RNase E is a key regulator of bacterial gene expression through its dual enzymatic functions.
Understanding RNase E's role is vital for comprehending bacterial pathogen survival and virulence.
The findings highlight RNase E as a potential target for antimicrobial strategies.