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The POT1–TPP1 telomere complex is a telomerase processivity factor
The crystal structure of a domain of human TPP1 reveals an oligonucleotide/oligosaccharide-binding fold that is structurally similar to the β-subunit of the telomere end-binding protein of a ciliated protozoan, suggesting that TPP1 is the missing β- subunit of human POT1 protein. Expand
Self-splicing RNA: Autoexcision and autocyclization of the ribosomal RNA intervening sequence of tetrahymena
- K. Kruger, P. Grabowski, A. Zaug, Julie Sands, D. Gottschling, T. Cech
- Medicine, Biology
- 1 November 1982
It is proposed that the IVS portion of the RNA has several enzyme-like properties that enable it to break and reform phosphodiester bonds and that enzymes, small nuclear RNAs and folding of the pre-rRNA into an RNP are unnecessary for these reactions. Expand
Saccharomyces cerevisiae telomerase is an Sm small nuclear ribonucleoprotein particle
It is shown that the Saccharomyces cerevisiae telomerase RNA has a 5′-2,2,7-trimethylguanosine (TMG) cap and a binding site for the Sm proteins, both hallmarks of small nuclear ribonucleoprotein particles (snRNPs) that are involved in nuclear messenger RNA splicing. Expand
Essential Regions of Saccharomyces cerevisiae Telomerase RNA: Separate Elements for Est1p and Est2p Interaction
The results support a role for the telomerase RNA serving as a scaffold for binding key protein subunits and having the RNA secured to the protein away from the template is proposed to facilitate the translocation of the RNA template through the active site. Expand
The TEL patch of telomere protein TPP1 mediates telomerase recruitment and processivity
- J. Nandakumar, C. Bell, Ina Weidenfeld, A. Zaug, L. Leinwand, T. Cech
- Biology, Medicine
- 16 October 2012
Seven separation-of-function mutants of human TPP1 are identified that retain full telomere-capping function in vitro and in vivo, yet are defective in binding human telomerase. Expand
In vitro splicing of the ribosomal RNA precursor of tetrahymena: Involvement of a guanosine nucleotide in the excision of the intervening sequence
It is proposed that Tetrahymena pre-rRNA splicing occurs by a phosphoester transferase mechanism where the guanosine cofactor provides the free 3' hydroxyl necessary to initiate a series of three transfers that results in splicing of the pre- rRNA and cyclization of the excised IVS. Expand
Human POT1 disrupts telomeric G-quadruplexes allowing telomerase extension in vitro.
- A. Zaug, E. Podell, T. Cech
- Biology, Medicine
- Proceedings of the National Academy of Sciences…
- 2 August 2005
It is shown that telomeric oligonucleotides, such as d[GGG(TTAGGG)(3)], which form intramolecular G-quadruplexes through Hoogsteen base-pairing, serve as only marginal primers for extension by recombinant human telomersase; telomerase stalls after every nucleotide addition. Expand
Functional interaction between telomere protein TPP1 and telomerase.
It is suggested that a sequence-specific interaction between TPP1 in the TPP1-POT1-telomeric DNA complex and the G100 region of the TEN domain of TERT is necessary for high-processivity telomerase action. Expand
The intervening sequence RNA of Tetrahymena is an enzyme.
The shortened form of the self-splicing ribosomal RNA intervening sequence of Tetrahymena thermophila acts as an enzyme in vitro that can act as an RNA polymerase, differing from the protein enzyme in that it uses an internal rather than an external template. Expand
Polyadenylation of telomerase RNA in budding yeast.
By putting the RNA under the control of an inducible promoter, it is shown that synthesis of the poly(A)+ RNA precedes that of thepoly(A)- fraction, which supports, but does not prove, a model in which all telomerase RNA is first polyadenylated and then rapidly processed to give the stable poly( A)-form. Expand