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Structure and function of echinoderm telomerase RNA.

Joshua D Podlevsky1, Yang Li1, Julian J-L Chen1

  • 1School of Molecular Sciences, Arizona State University, Tempe, Arizona 85287, USA.

RNA (New York, N.Y.)
|November 25, 2015
PubMed
Summary

Echinoderm telomerase RNA (TR) reveals unique structural features, including a novel eCR4/5 domain replacing the ancestral CR4/5 domain. This discovery offers insights into telomerase RNP evolution and function.

Keywords:
RNA structureevolutionribonucleoproteintelomeretemplate boundary

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Area of Science:

  • Molecular Biology
  • Evolutionary Biology
  • Biochemistry

Background:

  • Telomerase is a ribonucleoprotein (RNP) enzyme essential for maintaining telomere length, composed of telomerase RNA (TR) and telomerase reverse transcriptase (TERT).
  • TR secondary structures exhibit significant diversity across major taxa like ciliates, fungi, and vertebrates, with conserved template/pseudoknot and H/ACA domains.

Purpose of the Study:

  • To determine the comprehensive secondary structure of TR from echinoderms, marine invertebrates closely related to vertebrates.
  • To investigate the functional implications of echinoderm TR structure on telomerase activity and evolution.

Main Methods:

  • Phylogenetic comparative analysis of 16 TR sequences from three echinoderm classes.
  • Biochemical assays to assess the binding of echinoderm eCR4/5 domains to TERT and their effect on telomerase activity.

Main Results:

  • Echinoderm TR shares conserved template/pseudoknot and H/ACA domains with vertebrate TR but lacks the ancestral CR4/5 domain.
  • A novel eCR4/5 helical region in echinoderm TR is functionally equivalent to the CR4/5 domain, binding TERT and stimulating telomerase activity.
  • The echinoderm TR template/pseudoknot domain, when complexed with TERT, is sufficient for significant telomerase activity, unlike in vertebrates.
  • Echinoderm TR employs the P1.1 helix as a template boundary element, a mechanism conserved in ciliates and fungi.

Conclusions:

  • Echinoderm TR possesses a chimeric structure with unique features, including the eCR4/5 domain and a highly active template/pseudoknot domain.
  • These structural innovations likely facilitated rapid evolutionary changes in echinoderm TR.
  • The findings provide critical insights into the diverse evolutionary pathways of telomerase RNP structure and function.