LARP7-like protein Pof8 regulates telomerase assembly and poly(A)+TERRA expression in fission yeast.
basic_science · Level V
Where this comes from
- Record sourced from PubMed, PMID 29422503.
- Also identified by DOI 10.1038/s41467-018-02874-0 and PMC identifier 5805695.
- Licence recorded as CC BY.
- The licence permits redistribution, so the abstract is shown in full and the full text is available from the publisher.
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.
Medical subject headings
- RNA
- RNA Recognition Motif Proteins
- Schizosaccharomyces
- Schizosaccharomyces pombe Proteins
- Telomerase