A new role for proteins subunits of RNase P: stabilization of the telomerase holoenzyme
Authors:P. Daniela Garcia1 and Virginia A. Zakian2
1 Molecular Biosciences, The University of Texas at Austin, Austin, TX, 78712 USA.
2 Lewis-Sigler Institute, Princeton University, Princeton NJ 08544-1014 USA.
Keywords:
telomerase, telomere, RNase P, RNase MRP, telomerase RNA
Related Article(s)?
Garcia PD, Leach RW, Wadsworth GM, Choudhary K, Li H, Aviran S, Kim HD, Zakian VA (2020). Stability and Nuclear Localization of Yeast Telomerase Depend on Protein Components of RNase P/MRP. Nat Commun 11(1): 2173. , 10.1038/s41467-020-15875-9
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Conflict of interest statement:
The authors declare no conflict of interest.
Please cite this article as:
P. Daniela Garcia and Virginia A. Zakian (2020). A new role for proteins subunits of RNase P: stabilization of the telomerase holoenzyme. Microbial Cell 7(9): 250-254. doi: 10.15698/mic2020.09.730
© 2020 Garcia and Zakian. This is an open-access article released under the terms of the Creative Commons Attribution (CC BY) license, which allows the unrestricted use, distribution, and reproduc-tion in any medium, provided the original author and source are acknowledged.
Abstract:
RNase P, an RNA-protein complex, is essential for processing tRNAs. Three of the ten protein subunits of Saccharomyces cerevisiae RNase P (and a related complex, RNase MRP) co-purify with yeast telomerase, another RNA-protein complex. The three telomerase-associated proteins, Pop1, 6 and 7, bind to TLC1, the RNA subunit of telomerase. In a recent study (Garcia et al. Nat Commun), we used temperature sensitive alleles of the essential POP genes to determine their role in telomerase biogenesis. At permissive temperature, pop mutant cells grow normally, and the abundance of most proteins, including protein subunits of telomerase, is similar to wild type (WT). However, telomeres are short, and the amount of the mature telomerase holoenzyme is low. Unlike the RNA subunit of RNase MRP, TLC1 is more abundant in pop cells and properly folded, except at the Cs2a/TeSS domain where the Pop proteins bind. These defects correlate with defective movement of TLC1 from the cytoplasm, where it associates with telomerase proteins, back to the nucleus where it lengthens telomeres. Thus, Pop proteins are needed for the stable association of telomerase proteins with TLC1, and their reduction sequesters mature telomerase in the cytoplasm, away from its nuclear substrates.
doi: 10.15698/mic2020.09.730
Volume 7, pp. 250 to 254, published 17/06/2020.