LARP7-like protein Pof8 regulates telomerase assembly and poly(A)+TERRA expression in fission yeast

Amanda K. Mennie, Bettina A. Moser and Toru M. Nakamura ()
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Amanda K. Mennie: University of Illinois at Chicago
Bettina A. Moser: University of Illinois at Chicago
Toru M. Nakamura: University of Illinois at Chicago

Nature Communications, 2018, vol. 9, issue 1, 1-12

Abstract: Abstract Telomerase is a reverse transcriptase complex that ensures stable maintenance of linear eukaryotic chromosome ends by overcoming the end replication problem, posed by the inability of replicative DNA polymerases to fully replicate linear DNA. The catalytic subunit TERT must be assembled properly with its telomerase RNA for telomerase to function, and studies in Tetrahymena have established that p65, a La-related protein 7 (LARP7) family protein, utilizes its C-terminal xRRM domain to promote assembly of the telomerase ribonucleoprotein (RNP) complex. However, LARP7-dependent telomerase complex assembly has been considered as unique to ciliates that utilize RNA polymerase III to transcribe telomerase RNA. Here we show evidence that fission yeast Schizosaccharomyces pombe utilizes the p65-related protein Pof8 and its xRRM domain to promote assembly of RNA polymerase II-encoded telomerase RNA with TERT. Furthermore, we show that Pof8 contributes to repression of the transcription of noncoding RNAs at telomeres.

Date: 2018
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DOI: 10.1038/s41467-018-02874-0

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