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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...
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In vitro Reconstitution of the Active T. castaneum Telomerase
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Progress in Human and Tetrahymena Telomerase Structure Determination.

Henry Chan1, Yaqiang Wang1, Juli Feigon1

  • 1Department of Chemistry and Biochemistry, University of California, Los Angeles, California 90095-1569; email: feigon@mbi.ucla.edu , henrychan106@ucla.edu , yaqiang@mbi.ucla.edu.

Annual Review of Biophysics
|March 17, 2017
PubMed
Summary

Telomerase, an enzyme complex, maintains genome integrity by extending chromosome ends. Recent structural studies reveal how its components assemble and interact, offering insights into its function.

Keywords:
CSTH/ACA RNPelectron microscopyreplication protein Atelomerase RNAtelomerase reverse transcriptase

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Genetics

Background:

  • Telomerase is a crucial RNA-protein complex responsible for maintaining genome integrity.
  • It functions by extending the 3' ends of linear chromosomes using its telomerase reverse transcriptase (TERT) and telomerase RNA (TR) components.
  • Telomerase activity in vivo depends on its assembly with TERT, TR, and various telomere-associated proteins.

Purpose of the Study:

  • To review the structural basis of human and Tetrahymena telomerase activity.
  • To elucidate the assembly mechanisms of telomerase holoenzyme.
  • To understand telomerase interactions at telomeres.

Main Methods:

  • Analysis of cryo-electron microscopy (cryo-EM) data.
  • Structural biology techniques.
  • Review of existing literature on telomerase and telomere protein structures.

Main Results:

  • A 9-Å cryo-EM map of Tetrahymena telomerase holoenzyme provides a structural framework.
  • Insights into the assembly and functional interplay of TR, TERT, and associated proteins in both ciliate and vertebrate telomerases.
  • New understanding of telomerase interactions at telomeres.

Conclusions:

  • Structural insights are key to understanding telomerase function, assembly, and interactions.
  • The Tetrahymena telomerase structure serves as a model for diverse telomerase systems.
  • Further structural studies will continue to unravel telomerase mechanisms crucial for genome maintenance.