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Related Concept Videos

Mutations01:39

Mutations

Overview
Mutations01:35

Mutations

Mutations are changes in the sequence of DNA. These changes can occur spontaneously or they can be induced by exposure to environmental factors. Mutations can be characterized in a number of different ways: whether and how they alter the amino acid sequence of the protein, whether they occur over a small or large area of DNA, and whether they occur in somatic cells or germline cells.
Chromosomal Alterations Are Large-Scale Mutations
While point mutations are changes in a single nucleotide in...
Mutations01:39

Mutations

Overview
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...
Point and Frameshift Mutations01:30

Point and Frameshift Mutations

Point mutations are genetic alterations involving the change of a single nucleotide base pair in DNA. Depending on how the alteration affects protein synthesis, they can lead to various consequences.Point mutations fall into the following types:Silent mutations occur when a nucleotide change does not alter the amino acid sequence due to the redundancy of the genetic code. For instance, changing ACC to ACA still encodes threonine, leaving the protein function unaffected. This occurs because...
Mismatch Repair01:20

Mismatch Repair

Organisms are capable of detecting and fixing nucleotide mismatches that occur during DNA replication. This sophisticated process requires identifying the new strand and replacing the erroneous bases with correct nucleotides. Mismatch repair is coordinated by many proteins in both prokaryotes and eukaryotes.
The Mutator Protein Family Plays a Key Role in DNA Mismatch Repair
The human genome has more than 3 billion base pairs of DNA per cell. Prior to cell division, that vast amount of genetic...

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Following the Dynamics of Structural Variants in Experimentally Evolved Populations
04:52

Following the Dynamics of Structural Variants in Experimentally Evolved Populations

Published on: February 3, 2023

Mutation in TERT separates processivity from anchor-site function.

Arthur J Zaug1, Elaine R Podell, Thomas R Cech

  • 1Howard Hughes Medical Institute and Department of Chemistry and Biochemistry, University of Colorado, Boulder, Colorado 80309-0215, USA. Arthur.Zaug@Colorado.edu

Nature Structural & Molecular Biology
|July 22, 2008
PubMed
Summary
This summary is machine-generated.

Telomerase repeat-addition processivity (RAP) allows multiple DNA repeat synthesis. Mutants in Tetrahymena thermophila telomerase

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Gene-targeted Random Mutagenesis to Select Heterochromatin-destabilizing Proteasome Mutants in Fission Yeast

Published on: May 15, 2018

Area of Science:

  • Molecular Biology
  • Biochemistry
  • Genetics

Background:

  • Telomerase is a key enzyme responsible for maintaining telomere length.
  • Repeat-addition processivity (RAP) is a crucial feature of telomerase activity, enabling the synthesis of multiple telomeric DNA repeats without dissociation.
  • The N-terminal domain of telomerase reverse transcriptase plays a role in enzyme function.

Purpose of the Study:

  • To investigate the role of the N-terminal domain of Tetrahymena thermophila telomerase reverse transcriptase in repeat-addition processivity (RAP).
  • To understand the mechanism by which the N-terminal domain facilitates DNA translocation during telomere synthesis.

Main Methods:

  • Site-directed mutagenesis was used to create Leu14 mutants in the N-terminal domain of Tetrahymena thermophila telomerase reverse transcriptase.
  • Enzyme activity assays were performed to assess telomerase function, including processivity and anchor-site binding.
  • Analysis of DNA translocation mechanisms was inferred from the observed changes in RAP.

Main Results:

  • Leu14 mutants retained full telomerase activity and anchor-site function.
  • Despite retaining overall activity, Leu14 mutants lost repeat-addition processivity (RAP).
  • This dissociation between catalytic activity and RAP suggests a specific role for the N-terminal domain in facilitating DNA translocation.

Conclusions:

  • The N-terminal domain of telomerase reverse transcriptase is essential for repeat-addition processivity (RAP), but not for overall catalytic activity or anchor-site binding.
  • These findings provide insights into the molecular mechanisms underlying DNA translocation in telomerase.
  • The study suggests models for how this domain facilitates the movement of DNA during telomere elongation.