Literature DB >> 15351966

Adding to the ends: what makes telomerase processive and how important is it?

Neal F Lue1.   

Abstract

Telomerase is a cellular reverse transcriptase responsible for telomere maintenance in most organisms. It does so by adding telomere repeats onto pre-existing ends using an integral RNA component as template. Compared to "prototypical" reverse transcriptases, telomerase is unique in being able to repetitively copy a short templating RNA segment, thus adding multiple copies of the repeat to the DNA substrate following a single binding event. This uniquely processive property hints at the intricate conformational alterations that the enzyme must choreograph during its reaction cycles. Recent studies have identified distinct structural elements within both the RNA and protein components of telomerase that modulate enzyme processivity. Pharmacological and genetic analysis suggest that telomerase processivity is a significant determinant of telomere length. Because telomere maintenance and the lack thereof have been linked to tumor progression and aging, further investigation of telomerase processivity may lead to novel medical intervention strategies.

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Year:  2004        PMID: 15351966     DOI: 10.1002/bies.20093

Source DB:  PubMed          Journal:  Bioessays        ISSN: 0265-9247            Impact factor:   4.345


  33 in total

1.  RNA/DNA hybrid binding affinity determines telomerase template-translocation efficiency.

Authors:  Xiaodong Qi; Mingyi Xie; Andrew F Brown; Christopher J Bley; Joshua D Podlevsky; Julian J-L Chen
Journal:  EMBO J       Date:  2011-10-11       Impact factor: 11.598

2.  Tetrahymena telomerase protein p65 induces conformational changes throughout telomerase RNA (TER) and rescues telomerase reverse transcriptase and TER assembly mutants.

Authors:  Andrea J Berman; Anne R Gooding; Thomas R Cech
Journal:  Mol Cell Biol       Date:  2010-08-16       Impact factor: 4.272

3.  Protein-RNA interaction restricts telomerase from running through the stop sign.

Authors:  Linghe Xi; Thomas R Cech
Journal:  Nat Struct Mol Biol       Date:  2015-11       Impact factor: 15.369

4.  A physical and functional constituent of telomerase anchor site.

Authors:  Neal F Lue
Journal:  J Biol Chem       Date:  2005-05-18       Impact factor: 5.157

5.  Telomerase can act as a template- and RNA-independent terminal transferase.

Authors:  Neal F Lue; Dimitry Bosoy; Tara J Moriarty; Chantal Autexier; Brian Altman; Siyang Leng
Journal:  Proc Natl Acad Sci U S A       Date:  2005-06-30       Impact factor: 11.205

Review 6.  The biogenesis and regulation of telomerase holoenzymes.

Authors:  Kathleen Collins
Journal:  Nat Rev Mol Cell Biol       Date:  2006-07       Impact factor: 94.444

7.  Evolutionary patterns of non-coding RNAs.

Authors:  Athanasius F Bompfünewerer; Christoph Flamm; Claudia Fried; Guido Fritzsch; Ivo L Hofacker; Jörg Lehmann; Kristin Missal; Axel Mosig; Bettina Müller; Sonja J Prohaska; Bärbel M R Stadler; Peter F Stadler; Andrea Tanzer; Stefan Washietl; Christina Witwer
Journal:  Theory Biosci       Date:  2005-04       Impact factor: 1.919

8.  Does telomerase reverse transcriptase induce functional de-differentiation of human endothelial cells?

Authors:  Yvonne Baumer; Dorothee Funk; Burkhard Schlosshauer
Journal:  Cell Mol Life Sci       Date:  2010-03-30       Impact factor: 9.261

9.  Structural study of elements of Tetrahymena telomerase RNA stem-loop IV domain important for function.

Authors:  Rebecca J Richards; Haihong Wu; Lukas Trantirek; Catherine M O'Connor; Kathleen Collins; Juli Feigon
Journal:  RNA       Date:  2006-06-29       Impact factor: 4.942

10.  The N-terminus of hTERT contains a DNA-binding domain and is required for telomerase activity and cellular immortalization.

Authors:  David C F Sealey; Le Zheng; Michael A S Taboski; Jennifer Cruickshank; Mitsuhiko Ikura; Lea A Harrington
Journal:  Nucleic Acids Res       Date:  2009-12-23       Impact factor: 16.971

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