A putative cap binding protein and the methyl phosphate capping enzyme Bin3/MePCE function in telomerase biogenesis
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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 bio genesis. 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.
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Nature Communications, 13, Springer Nature, London, 2022, https://doi.org/10.1038/s41467-022-28545-9