A new role for proteins subunits of RNase P: stabilization of the telomerase holoenzyme
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...
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| Format: | Article |
| Language: | English |
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Shared Science Publishers OG
2020-06-01
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| Series: | Microbial Cell |
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| Online Access: | http://microbialcell.com/researcharticles/2020a-garcia-microbial-cell/ |
| _version_ | 1818835932037513216 |
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| author | P. Daniela Garcia Virginia A. Zakian |
| author_facet | P. Daniela Garcia Virginia A. Zakian |
| author_sort | P. Daniela Garcia |
| collection | DOAJ |
| description | 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. |
| first_indexed | 2024-12-19T02:58:34Z |
| format | Article |
| id | doaj.art-044800ec37254842a525a73e3ea2ee5e |
| institution | Directory Open Access Journal |
| issn | 2311-2638 |
| language | English |
| last_indexed | 2024-12-19T02:58:34Z |
| publishDate | 2020-06-01 |
| publisher | Shared Science Publishers OG |
| record_format | Article |
| series | Microbial Cell |
| spelling | doaj.art-044800ec37254842a525a73e3ea2ee5e2022-12-21T20:38:15ZengShared Science Publishers OGMicrobial Cell2311-26382020-06-017925025410.15698/mic2020.09.730A new role for proteins subunits of RNase P: stabilization of the telomerase holoenzymeP. Daniela Garcia0Virginia A. Zakian1Molecular Biosciences, The University of Texas at Austin, Austin, TX, 78712 USA.Lewis-Sigler Institute, Princeton University, Princeton NJ 08544-1014 USA.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.http://microbialcell.com/researcharticles/2020a-garcia-microbial-cell/telomerasetelomerernase prnase mrptelomerase rna |
| spellingShingle | P. Daniela Garcia Virginia A. Zakian A new role for proteins subunits of RNase P: stabilization of the telomerase holoenzyme Microbial Cell telomerase telomere rnase p rnase mrp telomerase rna |
| title | A new role for proteins subunits of RNase P: stabilization of the telomerase holoenzyme |
| title_full | A new role for proteins subunits of RNase P: stabilization of the telomerase holoenzyme |
| title_fullStr | A new role for proteins subunits of RNase P: stabilization of the telomerase holoenzyme |
| title_full_unstemmed | A new role for proteins subunits of RNase P: stabilization of the telomerase holoenzyme |
| title_short | A new role for proteins subunits of RNase P: stabilization of the telomerase holoenzyme |
| title_sort | new role for proteins subunits of rnase p stabilization of the telomerase holoenzyme |
| topic | telomerase telomere rnase p rnase mrp telomerase rna |
| url | http://microbialcell.com/researcharticles/2020a-garcia-microbial-cell/ |
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