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Article
Molecular analysis of PRC2 recruitment to DNA in chromatin and its inhibition by RNA
Biochemical reconstitution of PRC2 interactions with chromatinized templates demonstrates that protein-free linker DNA dominates the PRC2-nucleosome interaction, while RNA inhibits binding.
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Article
Inhibition of telomerase RNA decay rescues telomerase deficiency caused by dyskerin or PARN defects
New evidence that human telomerase RNA (hTR) degradation by EXOSC10 or DCP2 and XRN1 reduces telomerase activity when dyskerin is compromised suggests that RNA decay pathways may provide future therapeutic tar...
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Article
Protein-RNA interaction restricts telomerase from running through the stop sign
Telomerase is a unique reverse transcriptase in that it repetitively uses a short piece of its RNA component as template to synthesize DNA. A new crystal structure of a part of the Tetrahymena telomerase ribonucl...
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Article
Promiscuous RNA binding by Polycomb repressive complex 2
Polycomb repressive complex 2 (PRC2) is a histone methyltransferase required for epigenetic silencing during development and cancer, and it can be recruited to chromatin by long noncoding RNAs. In vitro binding s...
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Article
The RNA accordion model for template positioning by telomerase RNA during telomeric DNA synthesis
Telomerase uses its associated RNA as a template for processive addition of telomeric DNA repeats. Biochemistry and smFRET analysis are now used to investigate how the RNA template moves along the active site,...
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Article
Mutation in TERT separates processivity from anchor-site function
Repeat-addition processivity (RAP), that is, generating multiple DNA repeats from a single template without primer dissociation, is a key property of telomerase. In the Tetrahymena reverse-transcriptase component...
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Article
Triple-helix structure in telomerase RNA contributes to catalysis
Telomerase is responsible for replication of the ends of linear chromosomes in most eukaryotes. Its intrinsic RNA subunit provides the template for synthesis of telomeric DNA by the reverse-transcriptase (TERT...
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Article
Addendum: Crystal structure of the essential N-terminal domain of telomerase reverse transcriptase
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Article
Correction: Corrigendum: A miniature yeast telomerase RNA functions in vivo and reconstitutes activity in vitro
Nature Structural & Molecular Biology 12, 1072–1077 (2005); published online 20 November 2005; corrected after print 14 April 2006 In the supplementary information initially published online to accompany this ...
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Article
Crystal structure of the essential N-terminal domain of telomerase reverse transcriptase
Telomerase, a ribonucleoprotein enzyme, adds telomeric DNA repeats to the ends of linear chromosomes. Here we report the first high-resolution structure of any portion of the telomerase reverse transcriptase, ...
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Article
A miniature yeast telomerase RNA functions in vivo and reconstitutes activity in vitro
The ribonucleoprotein enzyme telomerase synthesizes DNA at the ends of chromosomes. Although the telomerase catalytic protein subunit (TERT) is well conserved, the RNA component is rapidly evolving in both siz...
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Article
Nurturing interdisciplinary research
The research in biology has been transformed by the products of interdisciplinary research. Here we explore why it is challenging for universities to bring biologists together with engineers, physicists and co...
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Article
Structure of human POT1 bound to telomeric single-stranded DNA provides a model for chromosome end-protection
The POT1 (protection of telomeres 1) protein binds the single-stranded overhang at the ends of chromosomes in diverse eukaryotes. It is essential for chromosome end-protection in the fission yeast Schizosaccharom...
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Article
Evolution of Tetrahymena ribozyme mutants with increased structural stability
Determining how large RNA molecules stabilize their tertiary structures is critical for understanding how they perform their biological functions. Here we use in vitro selection to identify active variants of the...
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Article
Representation of the secondary and tertiary structure of group I introns
Group I introns, which are widespread in nature, carry out RNA self–splicing. The secondary structure common to these introns was for the most part established a decade ago. Information about their higher orde...
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Article
Translocation of an RNA duplex on a ribozyme
RNA cleavage by the Tetrahymena ribozyme requires recognition of the reaction–site helix by the catalytic apparatus. This binding can occur in several registers, each of which results in reaction at a different n...