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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Cech, T. R. Lingner, J. |
| Description | Author Affiliation: Lingner J ( Howard Hughes Medical Institute, Department of Chemistry and Biochemistry, University of Colorado 80309-0215, USA.); |
| Abstract | Telomerase is a ribonucleoprotein enzyme that uses its internal RNA moiety as a template for synthesis of telomeric repeats at chromosome ends. Here we report the purification of telomerase from Euplotes aediculatus by affinity chromatography with antisense 2'-O-methyl oligonucleotides, a method that was developed for small nuclear ribonucleoprotein particles (snRNPs). Elution of bound ribonucleoprotein from the antisense oligonucleotide under nondenaturing conditions was achieved by a novel approach, using a displacement oligonucleotide. Polypeptides of 120 kDa and 43 kDa (a doublet) copurify with the active telomerase and appear stoichiometric with telomerase RNA. A simple model for DNA end replication predicts that after semiconservative DNA replication, telomerase will extend the newly synthesized, blunt-ended leading strand. We show that purified Euplotes telomerase has no activity with blunt-ended primers. Instead, efficient extension requires 4 to 6 single-stranded nucleotides at the 3' end. Therefore, this model predicts the existence of other activities such as helicases or nucleases that generate a single-stranded 3' end from a blunt end, thus activating the end for telomerase extension. |
| ISSN | 00278424 |
| e-ISSN | 10916490 |
| Journal | Proceedings of the National Academy of Sciences of the United States of America |
| Issue Number | 20 |
| Volume Number | 93 |
| Language | English |
| Publisher | National Academy of Sciences |
| Publisher Date | 1996-11-01 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Euplotes Enzymology Telomerase Isolation & Purification Animals Chromatography, Affinity DNA, Single-Stranded Metabolism Hydrogen Bonding Nucleic Acid Conformation Ribonucleoproteins Chemistry Substrate Specificity Research Support, Non-U.S. Gov't Multidisciplinary |
| Content Type | Text |
| Resource Type | Article |
| Subject | Multidisciplinary |
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