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Related Concept Videos

Telomeres and Telomerase02:41

Telomeres and Telomerase

In eukaryotic DNA replication, a single-stranded DNA fragment remains at the end of a chromosome after the removal of the final primer. This section of DNA cannot be replicated in the same manner as the rest of the strand because there is no 3’ end to which the newly synthesized DNA can attach. This non-replicated fragment results in gradual loss of the chromosomal DNA during each cell duplication. Additionally, it can induce a DNA damage response by enzymes that recognize single-stranded DNA.
Telomeres and Telomerase02:41

Telomeres and Telomerase

In eukaryotic DNA replication, a single-stranded DNA fragment remains at the end of a chromosome after the removal of the final primer. This section of DNA cannot be replicated in the same manner as the rest of the strand because there is no 3’ end to which the newly synthesized DNA can attach. This non-replicated fragment results in gradual loss of the chromosomal DNA during each cell duplication. Additionally, it can induce a DNA damage response by enzymes that recognize single-stranded DNA.
Bacterial Transcription01:53

Bacterial Transcription

RNA polymerase (RNAP) carries out DNA-dependent RNA synthesis in both bacteria and eukaryotes. Bacteria do not have a membrane-bound nucleus. So, transcription and translation occur simultaneously, on the same DNA template.
Transcription can be divided into three main stages, each involving distinct DNA sequences to guide the polymerase. These are:
The Replisome03:01

The Replisome

DNA replication is carried out by a large complex of proteins that act in a coordinated matter to achieve high-fidelity DNA replication. Together this complex is known as the DNA replication machinery or the replisome.
The synthesis of the leading and lagging strands is a highly coordinated process. To explain this, the “Trombone model” was proposed by Bruce Alberts in 1980. The DNA loop formation starts when a primer is synthesized on the parent lagging strand. The loop grows with the...
Translesion DNA Polymerases02:10

Translesion DNA Polymerases

Translesion (TLS) polymerases rescue stalled DNA polymerases at sites of damaged bases by replacing the replicative polymerase and installing a nucleotide across the damaged site. Doing so, TLS allows additional time for the cell to repair the damage before resuming regular DNA replication.
TLS polymerases are found in all three domains of life - archaea, bacteria, and eukaryotes. Of the different classes of TLS polymerases, members of the Y family are fitted with specialized structures that...
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...

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Related Experiment Video

Updated: May 23, 2026

Semi-quantitative Detection of RNA-dependent RNA Polymerase Activity of Human Telomerase Reverse Transcriptase Protein
08:26

Semi-quantitative Detection of RNA-dependent RNA Polymerase Activity of Human Telomerase Reverse Transcriptase Protein

Published on: June 12, 2018

Telomerase RNA biogenesis involves sequential binding by Sm and Lsm complexes.

Wen Tang1, Ram Kannan, Marco Blanchette

  • 1Howard Hughes Medical Institute, Kansas City, Missouri 64110, USA.

Nature
|March 27, 2012
PubMed
Summary
This summary is machine-generated.

Sm and Lsm proteins sequentially bind fission yeast telomerase RNA (TER1), guiding its maturation. This process involves spliceosome cleavage, 5'-cap hypermethylation by Tgs1, and protection of the 3'-end, crucial for telomerase biogenesis.

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Single-step Purification of Macromolecular Complexes Using RNA Attached to Biotin and a Photo-cleavable Linker
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Single-step Purification of Macromolecular Complexes Using RNA Attached to Biotin and a Photo-cleavable Linker

Published on: January 3, 2019

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Last Updated: May 23, 2026

Semi-quantitative Detection of RNA-dependent RNA Polymerase Activity of Human Telomerase Reverse Transcriptase Protein
08:26

Semi-quantitative Detection of RNA-dependent RNA Polymerase Activity of Human Telomerase Reverse Transcriptase Protein

Published on: June 12, 2018

Single-step Purification of Macromolecular Complexes Using RNA Attached to Biotin and a Photo-cleavable Linker
08:12

Single-step Purification of Macromolecular Complexes Using RNA Attached to Biotin and a Photo-cleavable Linker

Published on: January 3, 2019

Area of Science:

  • Molecular Biology
  • Biochemistry
  • Genetics

Background:

  • Telomerase counteracts DNA loss in eukaryotes, vital for cell stability.
  • Dysregulation of telomerase is linked to cancer and degenerative diseases.
  • Understanding telomerase biogenesis is key for therapeutic interventions.

Purpose of the Study:

  • To elucidate the sequential roles of Sm and Lsm proteins in fission yeast telomerase RNA (TER1) biogenesis.
  • To characterize the involvement of the spliceosome, Tgs1 methylase, and Sm/Lsm complexes in TER1 processing.

Main Methods:

  • Investigated Sm and Lsm2-8 complex association with TER1 precursor.
  • Analyzed spliceosomal cleavage and 5 -cap hypermethylation.
  • Assessed the role of these complexes in protecting mature TER1.

Main Results:

  • Demonstrated sequential binding of Sm ring and Lsm2-8 complex to TER1.
  • Showed Sm binding stimulates spliceosomal cleavage and Tgs1-mediated hypermethylation.
  • Confirmed Lsm2-8 complex promotes catalytic subunit association and 3 -end protection.

Conclusions:

  • Defined the step-by-step process of telomerase biogenesis in fission yeast.
  • Characterized novel roles for Sm, Lsm complexes, and Tgs1 in TER1 maturation.
  • Provided insights into the regulation of telomerase RNA processing.