메뉴 건너뛰기




Volumn 16, Issue 3, 2006, Pages 307-318

Structure and function of telomerase RNA

Author keywords

[No Author keywords available]

Indexed keywords

HOLOENZYME; PRIMER DNA; PROTEIN; PROTEIN CR4; PROTEIN CR5; RNA; TELOMERASE; UNCLASSIFIED DRUG;

EID: 33744799697     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.sbi.2006.05.005     Document Type: Review
Times cited : (166)

References (71)
  • 2
    • 1842813934 scopus 로고    scopus 로고
    • Telomerase RNA structure and function: implications for dyskeratosis congenita
    • Chen J.L., and Greider C.W. Telomerase RNA structure and function: implications for dyskeratosis congenita. Trends Biochem Sci 29 (2004) 183-192
    • (2004) Trends Biochem Sci , vol.29 , pp. 183-192
    • Chen, J.L.1    Greider, C.W.2
  • 4
    • 0022402513 scopus 로고
    • Identification of a specific telomere terminal transferase activity in Tetrahymena extracts
    • Greider C.W., and Blackburn E.H. Identification of a specific telomere terminal transferase activity in Tetrahymena extracts. Cell 43 (1985) 405-413
    • (1985) Cell , vol.43 , pp. 405-413
    • Greider, C.W.1    Blackburn, E.H.2
  • 5
    • 0024978857 scopus 로고
    • A telomeric sequence in the RNA of Tetrahymena telomerase required for telomere repeat synthesis
    • Greider C.W., and Blackburn E.H. A telomeric sequence in the RNA of Tetrahymena telomerase required for telomere repeat synthesis. Nature 337 (1989) 331-337
    • (1989) Nature , vol.337 , pp. 331-337
    • Greider, C.W.1    Blackburn, E.H.2
  • 7
    • 0141763835 scopus 로고    scopus 로고
    • Telomere maintenance and disease
    • Wong J.M.Y., and Collins K. Telomere maintenance and disease. Lancet 362 (2003) 983-988
    • (2003) Lancet , vol.362 , pp. 983-988
    • Wong, J.M.Y.1    Collins, K.2
  • 8
    • 0034598919 scopus 로고    scopus 로고
    • Secondary structure of vertebrate telomerase RNA
    • Chen J.L., Blasco M.A., and Greider C.W. Secondary structure of vertebrate telomerase RNA. Cell 100 (2000) 503-514
    • (2000) Cell , vol.100 , pp. 503-514
    • Chen, J.L.1    Blasco, M.A.2    Greider, C.W.3
  • 9
    • 0025944831 scopus 로고
    • A conserved secondary structure for telomerase RNA
    • Romero D.P., and Blackburn E.H. A conserved secondary structure for telomerase RNA. Cell 67 (1991) 343-353
    • (1991) Cell , vol.67 , pp. 343-353
    • Romero, D.P.1    Blackburn, E.H.2
  • 10
    • 3342875215 scopus 로고    scopus 로고
    • Structural elements required for association of the Saccharomyces cerevisiae telomerase RNA with the Est2 reverse transcriptase
    • The authors report the identification of an S. cerevisiae TER stem-loop and adjacent nucleotides that are required for interaction with the Est2 reverse transcriptase protein. They find that replacing this region with a minimal human TER pseudoknot results in a functional enzyme, suggesting that TERT recognizes a conserved structure.
    • Chappell A.S., and Lundblad V. Structural elements required for association of the Saccharomyces cerevisiae telomerase RNA with the Est2 reverse transcriptase. Mol Cell Biol 24 (2004) 7720-7736. The authors report the identification of an S. cerevisiae TER stem-loop and adjacent nucleotides that are required for interaction with the Est2 reverse transcriptase protein. They find that replacing this region with a minimal human TER pseudoknot results in a functional enzyme, suggesting that TERT recognizes a conserved structure.
    • (2004) Mol Cell Biol , vol.24 , pp. 7720-7736
    • Chappell, A.S.1    Lundblad, V.2
  • 11
    • 3142532677 scopus 로고    scopus 로고
    • A phylogenetically based secondary structure for the yeast telomerase RNA
    • The authors propose a secondary structure for yeast TER based on a phylogenetic comparative analysis of Saccharomyces species belonging to the 'sensu stricto' group coupled with in vitro enzymatic probing. The secondary structure includes an essential central domain containing two hairpins whose loops could form a potential tertiary interaction.
    • Dandjinou A.T., Levesque N., Larose S., Lucier J.F., Abou Elela S., and Wellinger R.J. A phylogenetically based secondary structure for the yeast telomerase RNA. Curr Biol 14 (2004) 1148-1158. The authors propose a secondary structure for yeast TER based on a phylogenetic comparative analysis of Saccharomyces species belonging to the 'sensu stricto' group coupled with in vitro enzymatic probing. The secondary structure includes an essential central domain containing two hairpins whose loops could form a potential tertiary interaction.
    • (2004) Curr Biol , vol.14 , pp. 1148-1158
    • Dandjinou, A.T.1    Levesque, N.2    Larose, S.3    Lucier, J.F.4    Abou Elela, S.5    Wellinger, R.J.6
  • 12
    • 6944242754 scopus 로고    scopus 로고
    • A universal telomerase RNA core structure includes structured motifs required for binding the telomerase reverse transcriptase protein
    • The authors propose a core domain for Saccharomyces and Kluyveromyces TER, based on phylogenetic comparison of TER sequences from several budding yeasts, that includes the template, a pseudoknot, a TBE and a template-enclosing helix. They further propose that this constitutes a minimal universal core domain for yeasts, vertebrates and ciliates.
    • Lin J., Ly H., Hussain A., Abraham M., Pearl S., Tzfati Y., Parslow T.G., and Blackburn E.H. A universal telomerase RNA core structure includes structured motifs required for binding the telomerase reverse transcriptase protein. Proc Natl Acad Sci USA 101 (2004) 14713-14718. The authors propose a core domain for Saccharomyces and Kluyveromyces TER, based on phylogenetic comparison of TER sequences from several budding yeasts, that includes the template, a pseudoknot, a TBE and a template-enclosing helix. They further propose that this constitutes a minimal universal core domain for yeasts, vertebrates and ciliates.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 14713-14718
    • Lin, J.1    Ly, H.2    Hussain, A.3    Abraham, M.4    Pearl, S.5    Tzfati, Y.6    Parslow, T.G.7    Blackburn, E.H.8
  • 13
    • 3042798454 scopus 로고    scopus 로고
    • Yeast telomerase RNA: a flexible scaffold for protein subunits
    • The authors propose that the secondary structure of S. cerevisiae TER is composed of a central catalytic core that contains the template and binds Est1p, and three long quasi-helical arms that bind Ku, Est1p and Sm proteins. These arms are proposed to act as flexible tethers for protein subunits. In support of this, they find that the Est1p-binding domain can be moved to three different locations with retention of telomerase activity in vivo.
    • Zappulla D.C., and Cech T.R. Yeast telomerase RNA: a flexible scaffold for protein subunits. Proc Natl Acad Sci USA 101 (2004) 10024-10029. The authors propose that the secondary structure of S. cerevisiae TER is composed of a central catalytic core that contains the template and binds Est1p, and three long quasi-helical arms that bind Ku, Est1p and Sm proteins. These arms are proposed to act as flexible tethers for protein subunits. In support of this, they find that the Est1p-binding domain can be moved to three different locations with retention of telomerase activity in vivo.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 10024-10029
    • Zappulla, D.C.1    Cech, T.R.2
  • 14
    • 6944256804 scopus 로고    scopus 로고
    • An emerging consensus for telomerase RNA structure
    • Chen J.L., and Greider C.W. An emerging consensus for telomerase RNA structure. Proc Natl Acad Sci USA 101 (2004) 14683-14684
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 14683-14684
    • Chen, J.L.1    Greider, C.W.2
  • 15
    • 0141557781 scopus 로고    scopus 로고
    • Comprehensive structure-function analysis of the core domain of human telomerase RNA
    • Ly H., Blackburn E.H., and Parslow T.G. Comprehensive structure-function analysis of the core domain of human telomerase RNA. Mol Cell Biol 23 (2003) 6849-6856
    • (2003) Mol Cell Biol , vol.23 , pp. 6849-6856
    • Ly, H.1    Blackburn, E.H.2    Parslow, T.G.3
  • 16
    • 18944391463 scopus 로고    scopus 로고
    • Biological and biochemical functions of RNA in the Tetrahymena telomerase holoenzyme
    • The authors investigate the functional role of the TBE, TRE, pseudoknot and stem-loop IV regions of T. thermophila TER in the context of the holoenzyme in vivo and in vitro. All of the elements except the pseudoknot are found be important for catalysis in vitro and telomere length maintenance in vivo.
    • Cunningham D.D., and Collins K. Biological and biochemical functions of RNA in the Tetrahymena telomerase holoenzyme. Mol Cell Biol 25 (2005) 4442-4454. The authors investigate the functional role of the TBE, TRE, pseudoknot and stem-loop IV regions of T. thermophila TER in the context of the holoenzyme in vivo and in vitro. All of the elements except the pseudoknot are found be important for catalysis in vitro and telomere length maintenance in vivo.
    • (2005) Mol Cell Biol , vol.25 , pp. 4442-4454
    • Cunningham, D.D.1    Collins, K.2
  • 17
    • 0037829618 scopus 로고    scopus 로고
    • A novel pseudoknot element is essential for the action of a yeast telomerase
    • Tzfati Y., Knight Z., Roy J., and Blackburn E.H. A novel pseudoknot element is essential for the action of a yeast telomerase. Genes Dev 17 (2003) 1779-1788
    • (2003) Genes Dev , vol.17 , pp. 1779-1788
    • Tzfati, Y.1    Knight, Z.2    Roy, J.3    Blackburn, E.H.4
  • 18
    • 0037457985 scopus 로고    scopus 로고
    • Mutations linked to dyskeratosis congenita cause changes in the structural equilibrium in telomerase RNA
    • Theimer C.A., Finger L.D., Trantirek L., and Feigon J. Mutations linked to dyskeratosis congenita cause changes in the structural equilibrium in telomerase RNA. Proc Natl Acad Sci USA 100 (2003) 449-454
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 449-454
    • Theimer, C.A.1    Finger, L.D.2    Trantirek, L.3    Feigon, J.4
  • 20
    • 0033754823 scopus 로고    scopus 로고
    • Dyskeratosis congenita in all its forms
    • Dokal I. Dyskeratosis congenita in all its forms. Br J Haematol 110 (2000) 768-779
    • (2000) Br J Haematol , vol.110 , pp. 768-779
    • Dokal, I.1
  • 21
    • 19444383162 scopus 로고    scopus 로고
    • Dyskeratosis congenita: telomerase, telomeres and anticipation
    • Marrone A., Walne A., and Dokal I. Dyskeratosis congenita: telomerase, telomeres and anticipation. Curr Opin Genet Dev 15 (2005) 249-257
    • (2005) Curr Opin Genet Dev , vol.15 , pp. 249-257
    • Marrone, A.1    Walne, A.2    Dokal, I.3
  • 22
    • 0035960043 scopus 로고    scopus 로고
    • The RNA component of telomerase is mutated in autosomal dominant dyskeratosis congenita
    • Vulliamy T., Marrone A., Goldman F., Dearlove A., Bessler M., Mason P.J., and Dokal I. The RNA component of telomerase is mutated in autosomal dominant dyskeratosis congenita. Nature 413 (2001) 432-435
    • (2001) Nature , vol.413 , pp. 432-435
    • Vulliamy, T.1    Marrone, A.2    Goldman, F.3    Dearlove, A.4    Bessler, M.5    Mason, P.J.6    Dokal, I.7
  • 23
    • 2442617343 scopus 로고    scopus 로고
    • Disease anticipation is associated with progressive telomere shortening in families with dyskeratosis congenita due to mutations in TERC
    • Vulliamy T., Marrone A., Szydlo R., Walne A., Mason P.J., and Dokal I. Disease anticipation is associated with progressive telomere shortening in families with dyskeratosis congenita due to mutations in TERC. Nat Genet 36 (2004) 447-449
    • (2004) Nat Genet , vol.36 , pp. 447-449
    • Vulliamy, T.1    Marrone, A.2    Szydlo, R.3    Walne, A.4    Mason, P.J.5    Dokal, I.6
  • 24
    • 15244358401 scopus 로고    scopus 로고
    • Functional characterization of telomerase RNA variants found in patients with hematologic disorders
    • The authors investigated the effects of twelve human TER mutations (including two new ones) associated with various diseases of the haemopoetic system on reconstituted telomerase activity in vivo. They made compensatory mutations to investigate the effect of the mutations on TER secondary structure. They found a good correlation between secondary structure perturbations and the degree of telomere shortening and telomerase activity in patient peripheral blood lymphocytes.
    • Ly H., Calado R.T., Allard P., Baerlocher G.M., Lansdorp P.M., Young N.S., and Parslow T.G. Functional characterization of telomerase RNA variants found in patients with hematologic disorders. Blood 105 (2005) 2332-2339. The authors investigated the effects of twelve human TER mutations (including two new ones) associated with various diseases of the haemopoetic system on reconstituted telomerase activity in vivo. They made compensatory mutations to investigate the effect of the mutations on TER secondary structure. They found a good correlation between secondary structure perturbations and the degree of telomere shortening and telomerase activity in patient peripheral blood lymphocytes.
    • (2005) Blood , vol.105 , pp. 2332-2339
    • Ly, H.1    Calado, R.T.2    Allard, P.3    Baerlocher, G.M.4    Lansdorp, P.M.5    Young, N.S.6    Parslow, T.G.7
  • 25
    • 23744511264 scopus 로고    scopus 로고
    • Identification and functional characterization of 2 variant alleles of the telomerase RNA template gene (TERC) in a patient with dyskeratosis congenita
    • Ly H., Schertzer M., Jastaniah W., Davis J., Yong S.L., Ouyang Q., Blackburn E.H., Parslow T.G., and Lansdorp P.M. Identification and functional characterization of 2 variant alleles of the telomerase RNA template gene (TERC) in a patient with dyskeratosis congenita. Blood 106 (2005) 1246-1252
    • (2005) Blood , vol.106 , pp. 1246-1252
    • Ly, H.1    Schertzer, M.2    Jastaniah, W.3    Davis, J.4    Yong, S.L.5    Ouyang, Q.6    Blackburn, E.H.7    Parslow, T.G.8    Lansdorp, P.M.9
  • 26
    • 33645508898 scopus 로고    scopus 로고
    • Mutations in dyskeratosis congenita: their impact on telomere length and the diversity of clinical presentation
    • This paper presents an extensive analysis of the correlations between clinical phenotype, disease mutations in TER, TERT and dyskerin, and telomere length using clinical and genetic information on 228 families in the DC Registry at Hammersmith Hospital in London.
    • Vulliamy T.J., Marrone A., Knight S.W., Walne A., Mason P.J., and Dokal I. Mutations in dyskeratosis congenita: their impact on telomere length and the diversity of clinical presentation. Blood 107 (2006) 2680-2685. This paper presents an extensive analysis of the correlations between clinical phenotype, disease mutations in TER, TERT and dyskerin, and telomere length using clinical and genetic information on 228 families in the DC Registry at Hammersmith Hospital in London.
    • (2006) Blood , vol.107 , pp. 2680-2685
    • Vulliamy, T.J.1    Marrone, A.2    Knight, S.W.3    Walne, A.4    Mason, P.J.5    Dokal, I.6
  • 28
    • 18844421369 scopus 로고    scopus 로고
    • Mutations in the reverse transcriptase component of telomerase (TERT) in patients with bone marrow failure
    • Vulliamy T.J., Walne A., Baskaradas A., Mason P.J., Marrone A., and Dokal I. Mutations in the reverse transcriptase component of telomerase (TERT) in patients with bone marrow failure. Blood Cells Mol Dis 34 (2005) 257-263
    • (2005) Blood Cells Mol Dis , vol.34 , pp. 257-263
    • Vulliamy, T.J.1    Walne, A.2    Baskaradas, A.3    Mason, P.J.4    Marrone, A.5    Dokal, I.6
  • 30
    • 14644435818 scopus 로고    scopus 로고
    • Structure of the human telomerase RNA pseudoknot reveals conserved tertiary interactions essential for function
    • The authors present the solution structure of a 47-nt pseudoknot from human TER, the largest region of TER to be determined to date. The tertiary interactions in the pseudoknot explain the sequence conservation in this region and the results of extensive biochemical and mutational studies, and reveal how disease mutations in this region would disrupt tertiary structure. The authors further present a thermodynamic analysis of mutant pseudoknots and show that telomerase activity is correlated with structural stability.
    • Theimer C.A., Blois C.A., and Feigon J. Structure of the human telomerase RNA pseudoknot reveals conserved tertiary interactions essential for function. Mol Cell 17 (2005) 671-682. The authors present the solution structure of a 47-nt pseudoknot from human TER, the largest region of TER to be determined to date. The tertiary interactions in the pseudoknot explain the sequence conservation in this region and the results of extensive biochemical and mutational studies, and reveal how disease mutations in this region would disrupt tertiary structure. The authors further present a thermodynamic analysis of mutant pseudoknots and show that telomerase activity is correlated with structural stability.
    • (2005) Mol Cell , vol.17 , pp. 671-682
    • Theimer, C.A.1    Blois, C.A.2    Feigon, J.3
  • 31
    • 15444376119 scopus 로고    scopus 로고
    • The structure of an enzyme-activating fragment of human telomerase RNA
    • The authors present the solution structure of the P6a-J6 region of the CR4/CR5 domain of human TER. The helix has a single-nucleotide bulge and an asymmetric internal loop that is conformationally flexible.
    • Leeper T.C., and Varani G. The structure of an enzyme-activating fragment of human telomerase RNA. RNA 11 (2005) 394-403. The authors present the solution structure of the P6a-J6 region of the CR4/CR5 domain of human TER. The helix has a single-nucleotide bulge and an asymmetric internal loop that is conformationally flexible.
    • (2005) RNA , vol.11 , pp. 394-403
    • Leeper, T.C.1    Varani, G.2
  • 32
    • 0032803237 scopus 로고    scopus 로고
    • Two inactive fragments of the integral RNA cooperate to assemble active telomerase with the human protein catalytic subunit (hTERT) in vitro
    • Tesmer V.M., Ford L.P., Holt S.E., Frank B.C., Yi X.M., Aisner D.L., Ouellette M., Shay J.W., and Wright W.E. Two inactive fragments of the integral RNA cooperate to assemble active telomerase with the human protein catalytic subunit (hTERT) in vitro. Mol Cell Biol 19 (1999) 6207-6216
    • (1999) Mol Cell Biol , vol.19 , pp. 6207-6216
    • Tesmer, V.M.1    Ford, L.P.2    Holt, S.E.3    Frank, B.C.4    Yi, X.M.5    Aisner, D.L.6    Ouellette, M.7    Shay, J.W.8    Wright, W.E.9
  • 33
    • 0033636897 scopus 로고    scopus 로고
    • Human telomerase activation requires two independent interactions between telomerase RNA and telomerase reverse transcriptase
    • Mitchell J.R., and Collins K. Human telomerase activation requires two independent interactions between telomerase RNA and telomerase reverse transcriptase. Mol Cell 6 (2000) 361-371
    • (2000) Mol Cell , vol.6 , pp. 361-371
    • Mitchell, J.R.1    Collins, K.2
  • 34
    • 10244222239 scopus 로고    scopus 로고
    • Heterozygous telomerase RNA mutations found in dyskeratosis congenita and aplastic anemia reduce telomerase activity via haploinsufficiency
    • Marrone A., Stevens D., Vulliamy T., Dokal I., and Mason P.J. Heterozygous telomerase RNA mutations found in dyskeratosis congenita and aplastic anemia reduce telomerase activity via haploinsufficiency. Blood 104 (2004) 3936-3942
    • (2004) Blood , vol.104 , pp. 3936-3942
    • Marrone, A.1    Stevens, D.2    Vulliamy, T.3    Dokal, I.4    Mason, P.J.5
  • 35
    • 20444374113 scopus 로고    scopus 로고
    • Functional analysis of the pseudoknot structure in human telomerase RNA
    • The authors present a mutational analysis of the conserved human TER pseudoknot designed to test whether there is conformational exchange between the pseudoknot and a stem 1 hairpin. They conclude that their mutational analysis supports a static pseudoknot structure. The authors show experimentally that telomerase activity does not require TER dimerization through the pseudoknot.
    • Chen J.L., and Greider C.W. Functional analysis of the pseudoknot structure in human telomerase RNA. Proc Natl Acad Sci USA 102 (2005) 8080-8085. The authors present a mutational analysis of the conserved human TER pseudoknot designed to test whether there is conformational exchange between the pseudoknot and a stem 1 hairpin. They conclude that their mutational analysis supports a static pseudoknot structure. The authors show experimentally that telomerase activity does not require TER dimerization through the pseudoknot.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 8080-8085
    • Chen, J.L.1    Greider, C.W.2
  • 36
    • 0037082416 scopus 로고    scopus 로고
    • Analysis of the structure of human telomerase RNA in vivo
    • Antal M., Boros E., Solymosy F., and Kiss T. Analysis of the structure of human telomerase RNA in vivo. Nucleic Acids Res 30 (2002) 912-920
    • (2002) Nucleic Acids Res , vol.30 , pp. 912-920
    • Antal, M.1    Boros, E.2    Solymosy, F.3    Kiss T4
  • 37
    • 0035723994 scopus 로고    scopus 로고
    • Functional multimerization of the human telomerase reverse transcriptase
    • Beattie T.L., Zhou W., Robinson M.O., and Harrington L. Functional multimerization of the human telomerase reverse transcriptase. Mol Cell Biol 21 (2001) 6151-6160
    • (2001) Mol Cell Biol , vol.21 , pp. 6151-6160
    • Beattie, T.L.1    Zhou, W.2    Robinson, M.O.3    Harrington, L.4
  • 38
    • 0036150238 scopus 로고    scopus 로고
    • Functional multimerization of human telomerase requires an RNA interaction domain in the N terminus of the catalytic subunit
    • Moriarty T.J., Huard S., Dupuis S., and Autexier C. Functional multimerization of human telomerase requires an RNA interaction domain in the N terminus of the catalytic subunit. Mol Cell Biol 22 (2002) 1253-1265
    • (2002) Mol Cell Biol , vol.22 , pp. 1253-1265
    • Moriarty, T.J.1    Huard, S.2    Dupuis, S.3    Autexier, C.4
  • 39
    • 0035796403 scopus 로고    scopus 로고
    • Human telomerase contains two cooperating telomerase RNA molecules
    • Wenz C., Enenkel B., Amacker M., Kelleher C., Damm K., and Lingner J. Human telomerase contains two cooperating telomerase RNA molecules. EMBO J 20 (2001) 3526-3534
    • (2001) EMBO J , vol.20 , pp. 3526-3534
    • Wenz, C.1    Enenkel, B.2    Amacker, M.3    Kelleher, C.4    Damm, K.5    Lingner, J.6
  • 40
    • 0030781067 scopus 로고    scopus 로고
    • Functionally interacting telomerase RNAs in the yeast telomerase complex
    • Prescott J., and Blackburn E.H. Functionally interacting telomerase RNAs in the yeast telomerase complex. Genes Dev 11 (1997) 2790-2800
    • (1997) Genes Dev , vol.11 , pp. 2790-2800
    • Prescott, J.1    Blackburn, E.H.2
  • 41
    • 0038305629 scopus 로고    scopus 로고
    • A role for a novel 'trans-pseudoknot' RNA-RNA interaction in the functional dimerization of human telomerase
    • Ly H., Xu L.F., Rivera M.A., Parslow T.G., and Blackburn E.H. A role for a novel 'trans-pseudoknot' RNA-RNA interaction in the functional dimerization of human telomerase. Genes Dev 17 (2003) 1078-1083
    • (2003) Genes Dev , vol.17 , pp. 1078-1083
    • Ly, H.1    Xu, L.F.2    Rivera, M.A.3    Parslow, T.G.4    Blackburn, E.H.5
  • 42
    • 27244458940 scopus 로고    scopus 로고
    • A human-Tetrahymena pseudoknot chimeric telomerase RNA reconstitutes a nonprocessive enzyme in vitro that is defective in telomere elongation
    • Marie-Egyptienne D.T., Cerone M.A., Londono-Vallejo J.A., and Autexier C. A human-Tetrahymena pseudoknot chimeric telomerase RNA reconstitutes a nonprocessive enzyme in vitro that is defective in telomere elongation. Nucleic Acids Res 33 (2005) 5446-5457
    • (2005) Nucleic Acids Res , vol.33 , pp. 5446-5457
    • Marie-Egyptienne, D.T.1    Cerone, M.A.2    Londono-Vallejo, J.A.3    Autexier, C.4
  • 43
    • 1942453903 scopus 로고    scopus 로고
    • Functional organization of repeat addition processivity and DNA synthesis determinants in the human telomerase multimer
    • The authors examined structural elements in human TER to determine their effects on DNA synthesis and/or repeat addition processivity using both direct and TRAP (telomeric repeat amplification protocol) assays with mutant TERs. They also determined that the RID1 domain of human TERT can be separated from the rest of the protein and act in trans.
    • Moriarty T.J., Marie-Egyptienne D.T., and Autexier C. Functional organization of repeat addition processivity and DNA synthesis determinants in the human telomerase multimer. Mol Cell Biol 24 (2004) 3720-3733. The authors examined structural elements in human TER to determine their effects on DNA synthesis and/or repeat addition processivity using both direct and TRAP (telomeric repeat amplification protocol) assays with mutant TERs. They also determined that the RID1 domain of human TERT can be separated from the rest of the protein and act in trans.
    • (2004) Mol Cell Biol , vol.24 , pp. 3720-3733
    • Moriarty, T.J.1    Marie-Egyptienne, D.T.2    Autexier, C.3
  • 44
    • 0345531140 scopus 로고    scopus 로고
    • Identification of a new RNA.RNA interaction site for human telomerase RNA (hTR): structural implications for hTR accumulation and a dyskeratosis congenita point mutation
    • Ren X., Gavory G., Li H., Ying L., Klenerman D., and Balasubramanian S. Identification of a new RNA.RNA interaction site for human telomerase RNA (hTR): structural implications for hTR accumulation and a dyskeratosis congenita point mutation. Nucleic Acids Res 31 (2003) 6509-6515
    • (2003) Nucleic Acids Res , vol.31 , pp. 6509-6515
    • Ren, X.1    Gavory, G.2    Li, H.3    Ying, L.4    Klenerman, D.5    Balasubramanian, S.6
  • 45
    • 0031029377 scopus 로고    scopus 로고
    • Telomerase RNA mutations in Saccharomyces cerevisiae alter telomerase action and reveal nonprocessivity in vivo and in vitro
    • Prescott J., and Blackburn E.H. Telomerase RNA mutations in Saccharomyces cerevisiae alter telomerase action and reveal nonprocessivity in vivo and in vitro. Genes Dev 11 (1997) 528-540
    • (1997) Genes Dev , vol.11 , pp. 528-540
    • Prescott, J.1    Blackburn, E.H.2
  • 46
    • 0026037255 scopus 로고
    • Developmentally programmed healing of chromosomes by telomerase in Tetrahymena
    • Yu G.L., and Blackburn E.H. Developmentally programmed healing of chromosomes by telomerase in Tetrahymena. Cell 67 (1991) 823-832
    • (1991) Cell , vol.67 , pp. 823-832
    • Yu, G.L.1    Blackburn, E.H.2
  • 47
    • 0037244006 scopus 로고    scopus 로고
    • N-terminal domain of yeast telomerase reverse transcriptase: recruitment of Est3p to the telomerase complex
    • Friedman K.L., Heit J.J., Long D.M., and Cech TR. N-terminal domain of yeast telomerase reverse transcriptase: recruitment of Est3p to the telomerase complex. Mol Biol Cell 14 (2003) 1-13
    • (2003) Mol Biol Cell , vol.14 , pp. 1-13
    • Friedman, K.L.1    Heit, J.J.2    Long, D.M.3    Cech TR4
  • 48
    • 0036118479 scopus 로고    scopus 로고
    • Essential regions of Saccharomyces cerevisiae telomerase RNA: separate elements for Est1p and Est2p interaction
    • Livengood A.J., Zaug A.J., and Cech T.R. Essential regions of Saccharomyces cerevisiae telomerase RNA: separate elements for Est1p and Est2p interaction. Mol Cell Biol 22 (2002) 2366-2374
    • (2002) Mol Cell Biol , vol.22 , pp. 2366-2374
    • Livengood, A.J.1    Zaug, A.J.2    Cech, T.R.3
  • 49
    • 0344875514 scopus 로고    scopus 로고
    • Tetrahymena telomerase is active as a monomer
    • Bryan T.M., Goodrich K.J., and Cech T.R. Tetrahymena telomerase is active as a monomer. Mol Biol Cell 14 (2003) 4794-4804
    • (2003) Mol Biol Cell , vol.14 , pp. 4794-4804
    • Bryan, T.M.1    Goodrich, K.J.2    Cech, T.R.3
  • 50
    • 11144235139 scopus 로고    scopus 로고
    • Processive utilization of the human telomerase template: lack of a requirement for template switching
    • The authors investigate the requirements for processive template usage by human telomerase through analysis of the effects of various mutations in the templating region on processivity and telomerase activity in vitro. They also show that template switching does not occur in a putative telomerase dimer.
    • Rivera M.A., and Blackburn E.H. Processive utilization of the human telomerase template: lack of a requirement for template switching. J Biol Chem 279 (2004) 53770-53781. The authors investigate the requirements for processive template usage by human telomerase through analysis of the effects of various mutations in the templating region on processivity and telomerase activity in vitro. They also show that template switching does not occur in a putative telomerase dimer.
    • (2004) J Biol Chem , vol.279 , pp. 53770-53781
    • Rivera, M.A.1    Blackburn, E.H.2
  • 51
    • 0344874270 scopus 로고    scopus 로고
    • YNMG tetraloop formation by a dyskeratosis congenita mutation in human telomerase RNA
    • Theimer C.A., Finger L.D., and Feigon J. YNMG tetraloop formation by a dyskeratosis congenita mutation in human telomerase RNA. RNA 9 (2003) 1446-1455
    • (2003) RNA , vol.9 , pp. 1446-1455
    • Theimer, C.A.1    Finger, L.D.2    Feigon J3
  • 52
    • 0038381556 scopus 로고    scopus 로고
    • The solution structure of an essential stem-loop of human telomerase RNA
    • Leeper T., Leulliot N., and Varani G. The solution structure of an essential stem-loop of human telomerase RNA. Nucleic Acids Res 31 (2003) 2614-2621
    • (2003) Nucleic Acids Res , vol.31 , pp. 2614-2621
    • Leeper, T.1    Leulliot, N.2    Varani, G.3
  • 53
    • 0037079673 scopus 로고    scopus 로고
    • A critical stem-loop structure in the CR4-CR5 domain of mammalian telomerase RNA
    • Chen J.L., Opperman K.K., and Greider C.W. A critical stem-loop structure in the CR4-CR5 domain of mammalian telomerase RNA. Nucleic Acids Res 30 (2002) 592-597
    • (2002) Nucleic Acids Res , vol.30 , pp. 592-597
    • Chen, J.L.1    Opperman, K.K.2    Greider, C.W.3
  • 54
    • 0346362327 scopus 로고    scopus 로고
    • Analysis of a long-range interaction between conserved domains of human telomerase RNA
    • The authors present gel mobility shift assays, mutational analyses and UV cross-linking experiments that indicate that the human TER p6.1 stem-loop interacts with the 11-nt templating domain.
    • Ueda C.T., and Roberts R.W. Analysis of a long-range interaction between conserved domains of human telomerase RNA. RNA 10 (2004) 139-147. The authors present gel mobility shift assays, mutational analyses and UV cross-linking experiments that indicate that the human TER p6.1 stem-loop interacts with the 11-nt templating domain.
    • (2004) RNA , vol.10 , pp. 139-147
    • Ueda, C.T.1    Roberts, R.W.2
  • 55
    • 2442651645 scopus 로고    scopus 로고
    • Holoenzyme proteins required for the physiological assembly and activity of telomerase
    • The authors report the isolation of epitope-tagged, endogenously assembled Tetrahymena telomerase by affinity purification. The complex is composed of TER, TERT, p20, p75 and two new proteins, p65 and p45. Both p65 and p45 are shown to be important for the maintenance of telomere length, and p65 for in vivo accumulation of TER.
    • Witkin K.L., and Collins K. Holoenzyme proteins required for the physiological assembly and activity of telomerase. Genes Dev 18 (2004) 1107-1118. The authors report the isolation of epitope-tagged, endogenously assembled Tetrahymena telomerase by affinity purification. The complex is composed of TER, TERT, p20, p75 and two new proteins, p65 and p45. Both p65 and p45 are shown to be important for the maintenance of telomere length, and p65 for in vivo accumulation of TER.
    • (2004) Genes Dev , vol.18 , pp. 1107-1118
    • Witkin, K.L.1    Collins, K.2
  • 56
    • 17844391288 scopus 로고    scopus 로고
    • A telomerase holoenzyme protein enhances telomerase RNA assembly with telomerase reverse transcriptase
    • Using recombinant p65, TERT and TER, the authors present data showing that p65 interacts with the 3′ stem region of Tetrahymena TER and enhances the assembly of TERT onto the TER. A conserved dinucleotide bulge is found to be important for p65-enhanced TERT RNP assembly.
    • Prathapam R., Witkin K.L., O'Connor C.M., and Collins K. A telomerase holoenzyme protein enhances telomerase RNA assembly with telomerase reverse transcriptase. Nat Struct Mol Biol 12 (2005) 252-257. Using recombinant p65, TERT and TER, the authors present data showing that p65 interacts with the 3′ stem region of Tetrahymena TER and enhances the assembly of TERT onto the TER. A conserved dinucleotide bulge is found to be important for p65-enhanced TERT RNP assembly.
    • (2005) Nat Struct Mol Biol , vol.12 , pp. 252-257
    • Prathapam, R.1    Witkin, K.L.2    O'Connor, C.M.3    Collins K4
  • 57
    • 20444481334 scopus 로고    scopus 로고
    • Two purified domains of telomerase reverse transcriptase reconstitute sequence-specific interactions with RNA
    • The authors report bacterial expression of two soluble domains of Tetrahymena TERT, the N-terminal domain and an RNA-binding domain. The interactions of these domains are mapped to specific elements of TER.
    • O'Connor C.M., Lai C.K., and Collins K. Two purified domains of telomerase reverse transcriptase reconstitute sequence-specific interactions with RNA. J Biol Chem 280 (2005) 17533-17539. The authors report bacterial expression of two soluble domains of Tetrahymena TERT, the N-terminal domain and an RNA-binding domain. The interactions of these domains are mapped to specific elements of TER.
    • (2005) J Biol Chem , vol.280 , pp. 17533-17539
    • O'Connor, C.M.1    Lai, C.K.2    Collins, K.3
  • 58
    • 33644745550 scopus 로고    scopus 로고
    • A novel RNA binding domain in Tetrahymena telomerase p65 initiates hierarchical assembly of telomerase holoenzyme
    • The authors identify four modular domains of p65, map their specific interactions with Tetrahymena TER and propose roles in telomerase holoenzyme assembly.
    • O'Connor C.M., and Collins K. A novel RNA binding domain in Tetrahymena telomerase p65 initiates hierarchical assembly of telomerase holoenzyme. Mol Cell Biol 26 (2006) 2029-2036. The authors identify four modular domains of p65, map their specific interactions with Tetrahymena TER and propose roles in telomerase holoenzyme assembly.
    • (2006) Mol Cell Biol , vol.26 , pp. 2029-2036
    • O'Connor, C.M.1    Collins, K.2
  • 59
    • 0028029818 scopus 로고
    • Architecture of telomerase RNA
    • Bhattacharyya A., and Blackburn E.H. Architecture of telomerase RNA. EMBO J 13 (1994) 5721-5731
    • (1994) EMBO J , vol.13 , pp. 5721-5731
    • Bhattacharyya, A.1    Blackburn, E.H.2
  • 60
    • 0035912746 scopus 로고    scopus 로고
    • A stem-loop of Tetrahymena telomerase RNA distant from the template potentiates RNA folding and telomerase activity
    • Sperger J.M., and Cech TR. A stem-loop of Tetrahymena telomerase RNA distant from the template potentiates RNA folding and telomerase activity. Biochemistry 40 (2001) 7005-7016
    • (2001) Biochemistry , vol.40 , pp. 7005-7016
    • Sperger, J.M.1    Cech TR2
  • 61
    • 23644461031 scopus 로고    scopus 로고
    • Soluble domains of telomerase reverse transcriptase identified by high-throughput screening
    • The authors present a high-throughput screen using a GFP-fusion system to isolate domains of T. thermophila TERT that are solubly expressed in E. coli. The N-terminal domain, which was purified and appeared folded by NMR analysis, and many domains that did not correspond to domains inferred from sequence alignment were identified.
    • Jacobs S.A., Podell E.R., Wuttke D.S., and Cech T.R. Soluble domains of telomerase reverse transcriptase identified by high-throughput screening. Protein Sci 14 (2005) 2051-2058. The authors present a high-throughput screen using a GFP-fusion system to isolate domains of T. thermophila TERT that are solubly expressed in E. coli. The N-terminal domain, which was purified and appeared folded by NMR analysis, and many domains that did not correspond to domains inferred from sequence alignment were identified.
    • (2005) Protein Sci , vol.14 , pp. 2051-2058
    • Jacobs, S.A.1    Podell, E.R.2    Wuttke, D.S.3    Cech, T.R.4
  • 63
    • 27444432533 scopus 로고    scopus 로고
    • Telomerase as a DNA-dependent DNA polymerase
    • Legassie J.D., and Jarstfer M.B. Telomerase as a DNA-dependent DNA polymerase. Biochemistry 44 (2005) 14191-14201
    • (2005) Biochemistry , vol.44 , pp. 14191-14201
    • Legassie, J.D.1    Jarstfer, M.B.2
  • 64
    • 33644864313 scopus 로고    scopus 로고
    • Structure of the Tetrahymena thermophila telomerase RNA helix II template boundary element
    • The authors report the solution structure of the T. thermophila TBE, which forms a hairpin with a structured pentaloop. The loop structure is compared with the same loop sequence found in 23S rRNA.
    • Richards R.J., Theimer C.A., Finger L.D., and Feigon J. Structure of the Tetrahymena thermophila telomerase RNA helix II template boundary element. Nucleic Acids Res 34 (2006) 816-825. The authors report the solution structure of the T. thermophila TBE, which forms a hairpin with a structured pentaloop. The loop structure is compared with the same loop sequence found in 23S rRNA.
    • (2006) Nucleic Acids Res , vol.34 , pp. 816-825
    • Richards, R.J.1    Theimer, C.A.2    Finger, L.D.3    Feigon, J.4
  • 65
    • 33644800744 scopus 로고    scopus 로고
    • Crystal structure of the essential N-terminal domain of telomerase reverse transcriptase
    • The authors report the crystal structure of the essential N-terminal domain (TEN) of T. thermophila TERT, which is the first structure of any domain of TERT and has a novel fold. They show that TEN interacts specifically with single-stranded telomeric DNA, consistent with a proposed role as the telomerase 'anchor site'. They also find that it binds TER in a non-sequence-specific manner via its C-terminal tail.
    • Jacobs S.A., Podell E.R., and Cech T.R. Crystal structure of the essential N-terminal domain of telomerase reverse transcriptase. Nat Struct Mol Biol 13 (2006) 218-225. The authors report the crystal structure of the essential N-terminal domain (TEN) of T. thermophila TERT, which is the first structure of any domain of TERT and has a novel fold. They show that TEN interacts specifically with single-stranded telomeric DNA, consistent with a proposed role as the telomerase 'anchor site'. They also find that it binds TER in a non-sequence-specific manner via its C-terminal tail.
    • (2006) Nat Struct Mol Biol , vol.13 , pp. 218-225
    • Jacobs, S.A.1    Podell, E.R.2    Cech, T.R.3
  • 66
    • 28544450412 scopus 로고    scopus 로고
    • A miniature yeast telomerase RNA functions in vivo and reconstitutes activity in vitro
    • The authors show that the 1157-nt S. cerevisiae TER can be reduced in size to 384-500 nt by deletion of flexible 'scaffolding arms' and still retain near wild-type function when reconstituted with TERT in vitro and when expressed in vivo. The mini-T telomerase should provide a good model system for investigating the roles of yeast telomerase accessory proteins.
    • Zappulla D.C., Goodrich K., and Cech T.R. A miniature yeast telomerase RNA functions in vivo and reconstitutes activity in vitro. Nat Struct Mol Biol 12 (2005) 1072-1077. The authors show that the 1157-nt S. cerevisiae TER can be reduced in size to 384-500 nt by deletion of flexible 'scaffolding arms' and still retain near wild-type function when reconstituted with TERT in vitro and when expressed in vivo. The mini-T telomerase should provide a good model system for investigating the roles of yeast telomerase accessory proteins.
    • (2005) Nat Struct Mol Biol , vol.12 , pp. 1072-1077
    • Zappulla, D.C.1    Goodrich, K.2    Cech, T.R.3
  • 67
    • 23944493620 scopus 로고    scopus 로고
    • Characterization of recombinant Saccharomyces cerevisiae telomerase core enzyme purified from yeast
    • The authors report purification of a reconstituted recombinant GST-Est2p-Tlc1 core yeast telomerase complex prepared from co-overexpressed GST-Est2p and Tlc1 in S. cerevisiae. The complex could synthesize one round of telomeric repeat.
    • Liao X.H., Zhang M.L., Yang C.P., Xu L.X., and Zhou J.Q. Characterization of recombinant Saccharomyces cerevisiae telomerase core enzyme purified from yeast. Biochem J 390 (2005) 169-176. The authors report purification of a reconstituted recombinant GST-Est2p-Tlc1 core yeast telomerase complex prepared from co-overexpressed GST-Est2p and Tlc1 in S. cerevisiae. The complex could synthesize one round of telomeric repeat.
    • (2005) Biochem J , vol.390 , pp. 169-176
    • Liao, X.H.1    Zhang, M.L.2    Yang, C.P.3    Xu, L.X.4    Zhou, J.Q.5
  • 68
    • 28544449371 scopus 로고    scopus 로고
    • The Cbf5-Nop10 complex is a molecular bracket that organizes box H/ACA RNPs
    • Hamma T., Reichow S.L., Varani G., and Ferre-D'Amare A.R. The Cbf5-Nop10 complex is a molecular bracket that organizes box H/ACA RNPs. Nat Struct Mol Biol 12 (2005) 1101-1107
    • (2005) Nat Struct Mol Biol , vol.12 , pp. 1101-1107
    • Hamma, T.1    Reichow, S.L.2    Varani, G.3    Ferre-D'Amare, A.R.4
  • 69
    • 29844442763 scopus 로고    scopus 로고
    • Structural study of the H/ACA snoRNP components Nop10p and the 3′ hairpin of U65 snoRNA
    • Khanna M., Wu H., Johansson C., Caizergues-Ferrer M., and Feigon J. Structural study of the H/ACA snoRNP components Nop10p and the 3′ hairpin of U65 snoRNA. RNA 12 (2006) 40-52
    • (2006) RNA , vol.12 , pp. 40-52
    • Khanna, M.1    Wu, H.2    Johansson, C.3    Caizergues-Ferrer, M.4    Feigon, J.5
  • 70
    • 30744445688 scopus 로고    scopus 로고
    • Crystal structure of a Cbf5-Nop10-Gar1 complex and implications in RNA-guided pseudouridylation and dyskeratosis congenita
    • Rashid R., Liang B., Baker D.L., Youssef O.A., He Y., Phipps K., Terns R.M., Terns M.P., and Li H. Crystal structure of a Cbf5-Nop10-Gar1 complex and implications in RNA-guided pseudouridylation and dyskeratosis congenita. Mol Cell 21 (2006) 249-260
    • (2006) Mol Cell , vol.21 , pp. 249-260
    • Rashid, R.1    Liang, B.2    Baker, D.L.3    Youssef, O.A.4    He, Y.5    Phipps, K.6    Terns, R.M.7    Terns, M.P.8    Li, H.9
  • 71
    • 0038392866 scopus 로고    scopus 로고
    • Distinct biogenesis pathways for human telomerase RNA and H/ACA small nucleolar RNAs
    • Fu D., and Collins K. Distinct biogenesis pathways for human telomerase RNA and H/ACA small nucleolar RNAs. Mol Cell 11 (2003) 1361-1372
    • (2003) Mol Cell , vol.11 , pp. 1361-1372
    • Fu, D.1    Collins, K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.