Nature Search

The Tetrahymena ribozyme acts like an RNA restriction endonuclease

Arthur J. Zaug
Michael D. Been
Thomas R. Cech
Research04 Dec 1986
Nature

Volume: 324, P: 429-433
Autocatalytic cyclization of an excised intervening sequence RNA is a cleavage–ligation reaction

Arthur J. Zaug
Paula J. Grabowski
Thomas R. Cech
Research17 Feb 1983
Nature

Volume: 301, P: 578-583
erratum: Saccharomyces cerevisiae telomerase is an Sm small nuclear ribonucleoprotein particle

Anita G. Seto
Arthur J. Zaug
Thomas R. Cech
Research23 Dec 1999
Nature

Volume: 402, P: 898
Erratum: The Tetrahymena ribozyme acts like an RNA restriction endonuclease

Arthur J. Zaug
Michael D. Been
Thomas R. Cech
Amendments and Corrections18 Feb 1987
Nature

Volume: 325, P: 646
Three-dimensional heteronuclear NMR studies of RNA

Edward P. Nikonowicz
Arthur Pardi
Research09 Jan 1992
Nature

Volume: 355, P: 184-186
The POT1–TPP1 telomere complex is a telomerase processivity factor

The structure of TPP1's oligonucleotide binding fold contains features that are particularly characteristic of TEBPβ. When the POT1–TPP1 complex is bound to telomeric DNA, it does not inhibit telomerase activity, as other telomere binding proteins do. Instead, the presence of POT1–TPP1 unexpectedly stimulates telomerase activity and processivity.

Feng Wang
Elaine R. Podell
Ming Lei
Research21 Jan 2007
Nature

Volume: 445, P: 506-510
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 of telomerase, a single amino acid mutation causes a profound and specific defect in RAP without altering enzymatic activity.

Arthur J Zaug
Elaine R Podell
Thomas R Cech
Research20 Jul 2008
Nature Structural & Molecular Biology

Volume: 15, P: 870-872
Ribozyme revealed

The first detailed look at the atomic structure of the hammerhead ribozyme provides a wealth of RNA structural information.

Arthur Pardi
News & Views01 Dec 1994
Nature Structural Biology

Volume: 1, P: 846-849
Telomerase RNA structural heterogeneity in living human cells detected by DMS-MaPseq

Telomerase assembles on a multi-domain RNA scaffold that must adopt a specific structure to function. Here, the authors reveal an alternative RNA conformation in living cells that disrupts telomerase activity, suggesting RNA misfolding may challenge proper telomerase assembly.

Nicholas M. Forino
Jia Zheng Woo
Michael D. Stone
ResearchOpen Access22 Jan 2025
Nature Communications

Volume: 16, P: 1-15
Reconstitution of a telomeric replicon organized by CST

The Polα–primase-associated CST complex organizes telomeric C-strand DNA synthesis, and, in combination with telomerase, it carries out complete replication of the single-stranded DNA overhang found at human telomeres.

Arthur J. Zaug
Karen J. Goodrich
Thomas R. Cech
ResearchOpen Access13 Jul 2022
Nature

Volume: 608, P: 819-825
Saccharomyces cerevisiae telomerase is an Sm small nuclear ribonucleoprotein particle

Anita G. Seto
Arthur J. Zaug
Thomas R. Cech
Research09 Sept 1999
Nature

Volume: 401, P: 177-180
Reconstitution of human shelterin complexes reveals unexpected stoichiometry and dual pathways to enhance telomerase processivity

The human shelterin complex protects telomere ends from being recognized as damaged DNA sites and regulates telomere length in conjunction with telomerase. Here the authors establish the stoichiometries of human shelterin complexes of various compositions and show shelterin provides dual pathways to stimulate telomerase processivity.

Ci Ji Lim
Arthur J. Zaug
Thomas R. Cech
ResearchOpen Access20 Oct 2017
Nature Communications

Volume: 8, P: 1-14
The TEL patch of telomere protein TPP1 mediates telomerase recruitment and processivity

Using separation-of-function mutations of TPP1 that inhibit telomerase binding while maintaining telomere capping, a region on the surface of TPP1, the TEL patch, is identified and found to be required for both binding telomerase and enhancing its processivity.

Jayakrishnan Nandakumar
Caitlin F. Bell
Thomas R. Cech
Research24 Oct 2012
Nature

Volume: 492, P: 285-289
Telomere shortening and loss of self-renewal in dyskeratosis congenita induced pluripotent stem cells

Luis F. Z. Batista
Matthew F. Pech
Steven E. Artandi
Research22 May 2011
Nature

Volume: 474, P: 399-402

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The Tetrahymena ribozyme acts like an RNA restriction endonuclease

Autocatalytic cyclization of an excised intervening sequence RNA is a cleavage–ligation reaction

erratum: Saccharomyces cerevisiae telomerase is an Sm small nuclear ribonucleoprotein particle

Erratum: The Tetrahymena ribozyme acts like an RNA restriction endonuclease

Three-dimensional heteronuclear NMR studies of RNA

The POT1–TPP1 telomere complex is a telomerase processivity factor

Mutation in TERT separates processivity from anchor-site function

Ribozyme revealed

Telomerase RNA structural heterogeneity in living human cells detected by DMS-MaPseq

Reconstitution of a telomeric replicon organized by CST

Saccharomyces cerevisiae telomerase is an Sm small nuclear ribonucleoprotein particle

Reconstitution of human shelterin complexes reveals unexpected stoichiometry and dual pathways to enhance telomerase processivity

The TEL patch of telomere protein TPP1 mediates telomerase recruitment and processivity

Telomere shortening and loss of self-renewal in dyskeratosis congenita induced pluripotent stem cells

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