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Related Concept Videos

LTR Retrotransposons03:08

LTR Retrotransposons

LTR retrotransposons are class I transposable elements with long terminal repeats flanking an internal coding region. These elements are less abundant in mammals compared to other class I transposable elements. About 8 percent of human genomic DNA comprises LTR retrotransposons. Some of the common examples of LTR retrotransposons are Ty elements in yeast and Copia elements in Drosophila.
The internal coding region of LTR retrotransposons and their mechanism of transposition closely resembles a...
Non-LTR Retrotransposons03:18

Non-LTR Retrotransposons

As the name suggests, non-LTR retrotransposons lack the long terminal repeats characteristic of the LTR retrotransposons. Additionally, both LTR and non-LTR retrotransposons use distinct mechanisms of mobilization. Non-LTR retrotransposons are further divided into two classes - Long interspersed nuclear elements (LINEs) and short interspersed nuclear elements (SINEs), both of which occur abundantly in most mammals, including humans. Some of the active non-LTR retrotransposons in humans are L1...
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...
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...
Retrovirus Life Cycles01:10

Retrovirus Life Cycles

Retroviruses have a single-stranded RNA genome that undergoes a special form of replication. Once the retrovirus has entered the host cell, an enzyme called reverse transcriptase synthesizes double-stranded DNA from the retroviral RNA genome. This DNA copy of the genome is then integrated into the host’s genome inside the nucleus via an enzyme called integrase. Consequently, the retroviral genome is transcribed into RNA whenever the host’s genome is transcribed, allowing the retrovirus to...
Retroviruses02:33

Retroviruses

Retroviruses and retrotransposons both insert copies of their genetic elements into the genome of the host cell. Thus, the viral genes are passed on when the host genome is replicated or translated. A typical retroviral DNA sequence contains 3-4 genes that encode the different proteins required for its structural assembly and function as a molecular parasite. This DNA is transcribed into a single mRNA, which is very similar in structure to conventional mRNAs, i.e., it is capped at the 5’...

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Related Experiment Video

Updated: Jun 13, 2026

Analysis of LINE-1 Retrotransposition at the Single Nucleus Level
11:52

Analysis of LINE-1 Retrotransposition at the Single Nucleus Level

Published on: April 23, 2016

R2 retrotransposons encode a self-cleaving ribozyme for processing from an rRNA cotranscript.

Danna G Eickbush1, Thomas H Eickbush

  • 1Department of Biology, University of Rochester, Rochester, NY 14627, USA. eick@mail.rochester.edu

Molecular and Cellular Biology
|April 28, 2010
PubMed
Summary
This summary is machine-generated.

The R2 retrotransposon in Drosophila uses a self-cleaving ribozyme to process its RNA. This mechanism, similar to the hepatitis delta virus ribozyme, evolved convergently in different Drosophila species.

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Artificial RNA Polymerase II Elongation Complexes for Dissecting Co-transcriptional RNA Processing Events

Published on: May 13, 2019

Area of Science:

  • Molecular Biology
  • Genetics
  • Evolutionary Biology

Background:

  • Non-long terminal repeat (non-LTR) retrotransposons, like R2, integrate into 28S ribosomal RNA (rRNA) genes in animals.
  • R2 element expression is typically cotranscribed with the host rRNA gene unit.

Purpose of the Study:

  • To investigate the mechanism of R2 element processing in the rRNA cotranscript.
  • To characterize the self-cleavage activity of the R2 element's 5' untranslated region.
  • To explore the evolutionary origins of the R2 ribozyme structure.

Main Methods:

  • In vitro RNA synthesis and self-cleavage assays.
  • Structural analysis of the R2 ribozyme, comparing it to the hepatitis delta virus (HDV) ribozyme.
  • Comparative sequence analysis of R2 elements across Drosophila species.

Main Results:

  • The 5' untranslated region of the R2 element in Drosophila simulans exhibits rapid and efficient self-cleavage of the 28S-R2 cotranscript.
  • The in vitro generated 5' end matches the in vivo processing site.
  • The R2 ribozyme folds into a double pseudoknot structure with significant nucleotide identity in the active site compared to the HDV ribozyme.
  • R2 elements from other Drosophila species also encode functional HDV-like ribozymes.

Conclusions:

  • The R2 element utilizes a ribozyme for precise RNA processing.
  • The structural and functional similarities between R2 and HDV ribozymes are a result of convergent evolution.
  • This study reveals an unexpected mechanism for retrotransposon RNA processing and its evolutionary trajectory.