Literature DB >> 10872448

Ciliate telomerase biochemistry.

K Collins1.   

Abstract

Telomerase is a cellular reverse transcriptase specialized for use of a template carried within the RNA component of the enzyme ribonucleoprotein complex. Substrates for telomerase are single-stranded oligonucleotides in vitro and chromosome ends in vivo. In vitro, a bound substrate is extended by an initial round of DNA synthesis on the internal RNA template and in some cases by multiple rounds of template copying before product dissociation. In vivo, de novo synthesis of one strand of a telomeric repeat sequence by telomerase balances the sequence loss resulting from incomplete replication of linear chromosome ends by RNA primer-requiring DNA polymerases. Telomerase biochemistry has been studied extensively by using partially purified cell extracts. Telomerase components are being identified and beginning to be produced in recombinant form. This review focuses on the enzyme mechanism of telomerases from ciliate species, thus far the most intensively studied systems.

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Year:  1999        PMID: 10872448     DOI: 10.1146/annurev.biochem.68.1.187

Source DB:  PubMed          Journal:  Annu Rev Biochem        ISSN: 0066-4154            Impact factor:   23.643


  42 in total

1.  Interference footprinting analysis of telomerase elongation complexes.

Authors:  S Benjamin; N Baran; H Manor
Journal:  Mol Cell Biol       Date:  2000-06       Impact factor: 4.272

2.  Template definition by Tetrahymena telomerase reverse transcriptase.

Authors:  M C Miller; J K Liu; K Collins
Journal:  EMBO J       Date:  2000-08-15       Impact factor: 11.598

3.  Telomerase recognizes its template by using an adjacent RNA motif.

Authors:  Michael C Miller; Kathleen Collins
Journal:  Proc Natl Acad Sci U S A       Date:  2002-05-07       Impact factor: 11.205

4.  Human telomerase domain interactions capture DNA for TEN domain-dependent processive elongation.

Authors:  Aaron R Robart; Kathleen Collins
Journal:  Mol Cell       Date:  2011-04-21       Impact factor: 17.970

5.  Studies on the minimal lengths required for DNA primers to be extended by the Tetrahymena telomerase: implications for primer positioning by the enzyme.

Authors:  Nava Baran; Yonit Haviv; Beena Paul; Haim Manor
Journal:  Nucleic Acids Res       Date:  2002-12-15       Impact factor: 16.971

6.  A conserved telomerase motif within the catalytic domain of telomerase reverse transcriptase is specifically required for repeat addition processivity.

Authors:  Neal F Lue; You-Chin Lin; I Saira Mian
Journal:  Mol Cell Biol       Date:  2003-12       Impact factor: 4.272

7.  Biological and biochemical functions of RNA in the tetrahymena telomerase holoenzyme.

Authors:  Doreen D Cunningham; Kathleen Collins
Journal:  Mol Cell Biol       Date:  2005-06       Impact factor: 4.272

8.  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

9.  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

10.  Oligomerization of the telomerase reverse transcriptase from Euplotes crassus.

Authors:  Libin Wang; Sierra R Dean; Dorothy E Shippen
Journal:  Nucleic Acids Res       Date:  2002-09-15       Impact factor: 16.971

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