Reconstitution of human shelterin complexes reveals unexpected stoichiometry and dual pathways to enhance telomerase processivity

Ci Ji Lim; Arthur J. Zaug; Hee Jin Kim; Thomas R. Cech

doi:10.1038/s41467-017-01313-w

Nature Communications (Oct 2017)

Reconstitution of human shelterin complexes reveals unexpected stoichiometry and dual pathways to enhance telomerase processivity

Ci Ji Lim,
Arthur J. Zaug,
Hee Jin Kim,
Thomas R. Cech

Affiliations

Ci Ji Lim: Howard Hughes Medical Institute, University of Colorado BioFrontiers Institute
Arthur J. Zaug: Howard Hughes Medical Institute, University of Colorado BioFrontiers Institute
Hee Jin Kim: Howard Hughes Medical Institute, University of Colorado BioFrontiers Institute
Thomas R. Cech: Howard Hughes Medical Institute, University of Colorado BioFrontiers Institute

DOI: https://doi.org/10.1038/s41467-017-01313-w
Journal volume & issue: Vol. 8, no. 1
pp. 1 – 14

Abstract

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The human shelterin complex protects telomere ends from being recognized as damaged DNA sites and regulates telomere length in conjunction with telomerase. Here the authors establish the stoichiometries of human shelterin complexes of various compositions and show shelterin provides dual pathways to stimulate telomerase processivity.

Published in Nature Communications

ISSN: 2041-1723 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science
Website: https://www.nature.com/ncomms/

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