A putative cap binding protein and the methyl phosphate capping enzyme Bin3/MePCE function in telomerase biogenesis

Diego J. Páez-Moscoso, David V. Ho, Lili Pan, Katie Hildebrand, Kristi L. Jensen, Michaella J. Levy, Laurence Florens and Peter Baumann ()
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Diego J. Páez-Moscoso: Johannes Gutenberg University
David V. Ho: Johannes Gutenberg University
Lili Pan: Johannes Gutenberg University
Katie Hildebrand: Stowers Institute for Medical Research
Kristi L. Jensen: Johannes Gutenberg University
Michaella J. Levy: Stowers Institute for Medical Research
Laurence Florens: Stowers Institute for Medical Research
Peter Baumann: Johannes Gutenberg University

Nature Communications, 2022, vol. 13, issue 1, 1-16

Abstract: Abstract Telomerase reverse transcriptase (TERT) and the noncoding telomerase RNA (TR) subunit constitute the core of telomerase. Additional subunits are required for ribonucleoprotein complex assembly and in some cases remain stably associated with the active holoenzyme. Pof8, a member of the LARP7 protein family is such a constitutive component of telomerase in fission yeast. Using affinity purification of Pof8, we have identified two previously uncharacterized proteins that form a complex with Pof8 and participate in telomerase biogenesis. Both proteins participate in ribonucleoprotein complex assembly and are required for wildtype telomerase activity and telomere length maintenance. One factor we named Thc1 (Telomerase Holoenzyme Component 1) shares structural similarity with the nuclear cap binding complex and the poly-adenosine ribonuclease (PARN), the other is the ortholog of the methyl phosphate capping enzyme (Bin3/MePCE) in metazoans and was named Bmc1 (Bin3/MePCE 1) to reflect its evolutionary roots. Thc1 and Bmc1 function together with Pof8 in recognizing correctly folded telomerase RNA and promoting the recruitment of the Lsm2-8 complex and the catalytic subunit to assemble functional telomerase.

Date: 2022
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DOI: 10.1038/s41467-022-28545-9

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