The methyl phosphate capping enzyme Bmc1/Bin3 is a stable component of the fission yeast telomerase holoenzyme

Jennifer Porat; Moaine El Baidouri; Jorg Grigull; Jean-Marc Deragon; Mark A. Bayfield

doi:10.1038/s41467-022-28985-3

Nature Communications (Mar 2022)

The methyl phosphate capping enzyme Bmc1/Bin3 is a stable component of the fission yeast telomerase holoenzyme

Jennifer Porat,
Moaine El Baidouri,
Jorg Grigull,
Jean-Marc Deragon,
Mark A. Bayfield

Affiliations

Jennifer Porat: Department of Biology, York University
Moaine El Baidouri: LGDP-UMR5096, Université de Perpignan Via Domitia
Jorg Grigull: Department of Mathematics and Statistics, York University
Jean-Marc Deragon: LGDP-UMR5096, Université de Perpignan Via Domitia
Mark A. Bayfield: Department of Biology, York University

DOI: https://doi.org/10.1038/s41467-022-28985-3
Journal volume & issue: Vol. 13, no. 1
pp. 1 – 14

Abstract

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There exists a remarkable evolutionary breadth of telomerase holoenzyme components among eukaryotes. Here the authors report that the fission yeast methyl phosphate capping enzyme Bin3/Bmc1 regulates telomerase activity by promoting holoenzyme formation.

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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