Structural biology of telomerase and its interaction at telomeres

Curr Opin Struct Biol. 2017 Dec:47:77-87. doi: 10.1016/j.sbi.2017.06.010. Epub 2017 Jul 18.

Abstract

Telomerase is an RNP that synthesizes the 3' ends of linear chromosomes and is an important regulator of telomere length. It contains a single long non-coding telomerase RNA (TER), telomerase reverse transcriptase (TERT), and other proteins that vary among organisms. Recent progress in structural biology of telomerase includes reports of the first cryo-electron microscopy structure of telomerase, from Tetrahymena, new crystal structures of TERT domains, telomerase RNA structures and models, and identification in Tetrahymena telomerase holoenzyme of human homologues of telomere-associated proteins that have provided a more unified view of telomerase interaction at telomeres as well as insights into the role of telomerase RNA in activity and assembly.

Publication types

  • Review

MeSH terms

  • Cryoelectron Microscopy
  • Models, Biological
  • Models, Molecular
  • Nucleic Acid Conformation
  • Protein Binding
  • Protein Conformation
  • Protein Interaction Domains and Motifs
  • Structure-Activity Relationship
  • Telomerase / chemistry*
  • Telomerase / metabolism*
  • Telomere / chemistry*
  • Telomere / genetics
  • Telomere / metabolism*

Substances

  • Telomerase