Cited by 10Telomeres, Telomerase, and SenescenceNuclear Structure and FunctionGenetics, Aging, and Longevity in Model Organisms

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

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Páez-Moscoso, Diego J., Ho, David V., Pan, Lili, Hildebrand, Katie, Jensen, Kristi L., Levy, Michaella J., Florens, Laurence, Baumann, Peter·2022·Nature Communications

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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 biogenesis. Both proteins participate in ribonucleoprotein complex assembly and are required for wildtype telomerase activity and telomere length maintenance. One factor we named Thc1 ( T elomerase H oloenzyme C omponent 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 ( B in3/ M eP C E 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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Authors
Páez-Moscoso, D. J., Ho, D. V., Pan, L., Hildebrand, K., Jensen, K. L., Levy, M. J., Florens, L., & Baumann, P.
Affiliations
  • Stowers Institute for Medical Research (US)
  • Johannes Gutenberg University Mainz (DE)
Corresponding author
Baumann, Peter
Venue
Nature Communications
Published
2022-02-25
Volume
13
Issue
1
Pages
1067-1067
ISSN
2041-1723 (ISSN-L)
OpenAlex
W4221125806
Cited by
10
References
3
Citations by year
2025: 2 · 2024: 1 · 2023: 5 · 2022: 2
FWCI
1.55
Type
journal article
Language
en
Open access
Locations
  • Nature Communications (publishedVersion, cc-by)
  • PubMed Central (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
Funders
  • Alexander von Humboldt-Stiftung
  • Howard Hughes Medical Institute
  • Stowers Institute for Medical Research
Topics
  • Health Sciences › Medicine › Physiology › Telomeres, Telomerase, and Senescence
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Nuclear Structure and Function
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Aging › Genetics, Aging, and Longevity in Model Organisms
Keywords
telomerase biogenesis, telomerase reverse transcriptase, telomerase RNA, cap-binding protein, telomere maintenance, Schizosaccharomyces pombe, protein complex formation
MeSH terms
Phosphates, Protein Binding, RNA, Schizosaccharomyces, Telomere, Telomerase, Holoenzymes, RNA Cap-Binding Proteins

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