File(s) stored somewhere else

Please note: Linked content is NOT stored on University of Illinois at Chicago and we can't guarantee its availability, quality, security or accept any liability.

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

journal contribution
posted on 22.11.2022, 23:51 authored by Amanda K Mennie, Bettina MoserBettina Moser, Toru NakamuraToru Nakamura
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.

Funding

Roles of Checkpoint and DNA Repair Proteins in Fission Yeast Telomere Maintenance | Funder: National Institutes of Health (National Institute of General Medical Sciences) | Grant ID: R01GM078253

History

Citation

Mennie, A. K., Moser, B. A.Nakamura, T. M. (2018). LARP7-like protein Pof8 regulates telomerase assembly and poly(A)+TERRA expression in fission yeast. Nature Communications, 9(1), 586-. https://doi.org/10.1038/s41467-018-02874-0

Publisher

Springer Nature

Language

en

issn

2041-1723