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Related Concept Videos

Bacterial RNA Polymerase00:43

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...
Eukaryotic RNA Polymerases00:58

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...
Ribosomal RNA Synthesis02:53

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,...
Ribozymes02:47

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 be...
Ribosome Profiling02:24

Ribosome Profiling

Ribosome profiling or ribo-sequencing is a deep sequencing technique that produces a snapshot of active translation in a cell. It selectively sequences the mRNAs protected by ribosomes to get an insight into a cell’s translation landscape at any given point in time.
Applications of ribosome profiling
Ribosome profiling has many applications, including in vivo monitoring of translation inside a particular organ or tissue type and quantifying new protein synthesis levels.
The technique helps...
Transcription Initiation01:47

Transcription Initiation

Initiation is the first step of transcription in eukaryotes. Prokaryotic RNA Polymerase (RNAP) can bind to the template DNA and start transcribing. On the other hand, transcription in eukaryotes requires additional proteins, called transcription factors, to first bind to the promoter region in the DNA template. This binding helps recruit the specific RNAP that can assemble on the DNA and start transcription.
The promoters and enhancers and their accessory proteins allow tight regulation of...

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Related Experiment Video

Updated: Jul 19, 2026

Analyzing Gene Expression from Marine Microbial Communities using Environmental Transcriptomics
13:51

Analyzing Gene Expression from Marine Microbial Communities using Environmental Transcriptomics

Published on: February 18, 2009

The rne gene and ribonuclease E

A Miczak1, D Apirion

  • 1Department of Molecular Microbiology, Washington University Medical School, St Louis, MO 63110.

Biochimie
|January 1, 1993
PubMed
Summary

The cloned rne+ gene codes for RNase E, an essential enzyme. Post-translational modifications in cells may affect RNase E

Area of Science:

  • Molecular Biology
  • Enzymology
  • Gene Expression

Background:

  • RNase E is a crucial enzyme involved in RNA processing.
  • Understanding the genetic basis and regulation of RNase E is important for bacterial physiology.

Purpose of the Study:

  • To identify and characterize the structural gene for RNase E.
  • To investigate the properties and potential modifications of the RNase E protein.

Main Methods:

  • Gene cloning and complementation analysis of temperature-sensitive RNase E mutations.
  • In vitro transcription and translation of the cloned rne+ gene.
  • Assay of RNase E activity in cell-free extracts.
  • Analysis of RNase E thermolability under different cellular conditions.

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Main Results:

  • The cloned rne+ gene successfully complemented RNase E mutations and directed polypeptide synthesis.
  • RNA transcribed from the rne+ gene directed the synthesis of a polypeptide identical in size to the in vivo RNase E product.
  • Cell-free extracts programmed with rne+ RNA exhibited RNase E activity.
  • The in vivo product of the cloned RNase E gene was more thermolabile than the chromosomal gene product.
  • Treatment with chloramphenicol suggested post-translational modification(s) of RNase E in vivo.

Conclusions:

  • The rne gene is confirmed as the structural gene for RNase E.
  • RNase E likely undergoes post-translational modifications in vivo, influencing its stability.
  • Further research into these modifications could reveal new regulatory mechanisms for RNase E function.