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Pof8 is a La-related protein and a constitutive component of telomerase in fission yeast

Author

Listed:
  • Diego J. Páez-Moscoso

    (Stowers Institute for Medical Research)

  • Lili Pan

    (Stowers Institute for Medical Research)

  • Rutendo F. Sigauke

    (Stowers Institute for Medical Research)

  • Morgan R. Schroeder

    (Stowers Institute for Medical Research)

  • Wen Tang

    (Stowers Institute for Medical Research
    University of Massachusetts Medical School)

  • Peter Baumann

    (Stowers Institute for Medical Research
    Howard Hughes Medical Institute
    University of Kansas Medical Center
    Johannes Gutenberg University)

Abstract

Telomerase reverse transcriptase (TERT) and the non-coding telomerase RNA subunit (TR) constitute the core of telomerase. Here we now report that the putative F-box protein Pof8 is also a constitutive component of active telomerase in fission yeast. Pof8 functions in a hierarchical assembly pathway by promoting the binding of the Lsm2-8 complex to telomerase RNA, which in turn promotes binding of the catalytic subunit. Loss of Pof8 reduces TER1 stability, causes a severe assembly defect, and results in critically short telomeres. Structure profile searches identified similarities between Pof8 and telomerase subunits from ciliated protozoa, making Pof8 next to TERT the most widely conserved telomerase subunits identified to date.

Suggested Citation

  • Diego J. Páez-Moscoso & Lili Pan & Rutendo F. Sigauke & Morgan R. Schroeder & Wen Tang & Peter Baumann, 2018. "Pof8 is a La-related protein and a constitutive component of telomerase in fission yeast," Nature Communications, Nature, vol. 9(1), pages 1-11, December.
    • Handle: RePEc:nat:natcom:v:9:y:2018:i:1:d:10.1038_s41467-017-02284-8
    DOI: 10.1038/s41467-017-02284-8
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