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  1. No Access

    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.

    Xueyin Wang, Richard D Paucek, Anne R Gooding in Nature Structural & Molecular Biology (2017)

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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...

    Siddharth Shukla, Jens C Schmidt in Nature Structural & Molecular Biology (2016)

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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...

    Linghe **, Thomas R Cech in Nature Structural & Molecular Biology (2015)

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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...

    Chen Davidovich, Leon Zheng, Karen J Goodrich in Nature Structural & Molecular Biology (2013)

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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,...

    Andrea J Berman, Benjamin M Akiyama in Nature Structural & Molecular Biology (2011)

  6. No Access

    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...

    Arthur J Zaug, Elaine R Podell, Thomas R Cech in Nature Structural & Molecular Biology (2008)

  7. No Access

    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...

    Feng Qiao, Thomas R Cech in Nature Structural & Molecular Biology (2008)

  8. Article

    Addendum: Crystal structure of the essential N-terminal domain of telomerase reverse transcriptase

    Steven A Jacobs, Elaine R Podell, Thomas R Cech in Nature Structural & Molecular Biology (2007)

  9. 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 ...

    David C Zappulla, Karen Goodrich, Thomas R Cech in Nature Structural & Molecular Biology (2006)

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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, ...

    Steven A Jacobs, Elaine R Podell, Thomas R Cech in Nature Structural & Molecular Biology (2006)

  11. No Access

    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...

    David C Zappulla, Karen Goodrich, Thomas R Cech in Nature Structural & Molecular Biology (2005)

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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...

    Thomas R Cech, Gerald M Rubin in Nature Structural & Molecular Biology (2004)

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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...

    Ming Lei, Elaine R Podell, Thomas R Cech in Nature Structural & Molecular Biology (2004)

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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...

    Feng Guo, Thomas R. Cech in Nature Structural Biology (2002)

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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...

    Thomas R. Cech, Simon H. Damberger, Robin R. Gutell in Nature Structural Biology (1994)

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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...

    Scott A. Strobel, Thomas R. Cech in Nature Structural Biology (1994)