Abstract 2789 Tudor domain-containing protein SPF30 regulates telomerase activity by modulating TERC processing via interaction with MTR4-RNA exosome

Nuclear RNA exosome is a 3′-5′ exonuclease complex functioning in degradation or processing of many species of RNAs, including rRNAs, snRNAs and snoRNAs, in collaboration with an RNA helicase MTR4. Recently, we have found that SPF30/SMNDC1, a Tudor domain-containing protein with potential binding to dimethylarginine-modified proteins, interacts with the MTR4-RNA exosome complex under regulation of a chaperone-like AAA-ATPase NVL2. The RNA component of human telomerase (TERC/hTR) is biosynthesized from a larger precursor through trimming of 3′-extended sequence.