메뉴 건너뛰기




Volumn 452, Issue 3, 2014, Pages 436-442

Solution structure of telomere binding domain of AtTRB2 derived from Arabidopsis thaliana

Author keywords

Arabidopsis thaliana telomere repeat binding factor 2 (AtTRB2); NMR spectroscopy; Single Myb Histone (SMH); Solution structure; Telomere associated protein

Indexed keywords

TELOMERIC REPEAT BINDING FACTOR 2; ARABIDOPSIS PROTEIN; ARGININE; DNA; PROTEIN BINDING; RECOMBINANT PROTEIN; TELOMERE BINDING PROTEIN; TRB2 PROTEIN, ARABIDOPSIS; TRYPTOPHAN; VALINE;

EID: 84907535055     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2014.08.095     Document Type: Article
Times cited : (6)

References (41)
  • 1
    • 0025222442 scopus 로고
    • RAP1 protein interacts with yeast telomeres in vivo: Overproduction alters telomere structure and decreases chromosome stability
    • M.N. Conrad, J.H. Wright, A.J. Wolf, and V.A. Zakian RAP1 protein interacts with yeast telomeres in vivo: overproduction alters telomere structure and decreases chromosome stability Cell 63 1990 739 750
    • (1990) Cell , vol.63 , pp. 739-750
    • Conrad, M.N.1    Wright, J.H.2    Wolf, A.J.3    Zakian, V.A.4
  • 2
    • 0024281368 scopus 로고
    • Isolation of a higher eukaryotic telomere from Arabidopsis thaliana
    • E.J. Richards, and F.M. Ausubel Isolation of a higher eukaryotic telomere from Arabidopsis thaliana Cell 53 1988 127 136
    • (1988) Cell , vol.53 , pp. 127-136
    • Richards, E.J.1    Ausubel, F.M.2
  • 3
    • 0034020630 scopus 로고    scopus 로고
    • Mammalian telomeres and telomerase
    • K. Collins Mammalian telomeres and telomerase Curr. Opin. Cell Biol. 12 2000 378 383
    • (2000) Curr. Opin. Cell Biol. , vol.12 , pp. 378-383
    • Collins, K.1
  • 4
    • 0031010342 scopus 로고    scopus 로고
    • A survey of telomerase activity in human cancer
    • J.W. Shay, and S. Bacchetti A survey of telomerase activity in human cancer Eur. J. Cancer 33 1997 787 791
    • (1997) Eur. J. Cancer , vol.33 , pp. 787-791
    • Shay, J.W.1    Bacchetti, S.2
  • 5
    • 0029872174 scopus 로고    scopus 로고
    • Telomerase activity in human germline and embryonic tissues and cells
    • W.E. Wright, M.A. Piatyszek, W.E. Rainey, W. Byrd, and J.W. Shay Telomerase activity in human germline and embryonic tissues and cells Dev. Genet. 18 1996 173 179
    • (1996) Dev. Genet. , vol.18 , pp. 173-179
    • Wright, W.E.1    Piatyszek, M.A.2    Rainey, W.E.3    Byrd, W.4    Shay, J.W.5
  • 7
    • 0034705495 scopus 로고    scopus 로고
    • Molecular biology. Telomeres keep on rappin
    • V. Lundblad Molecular biology. Telomeres keep on rappin Science 288 2000 2141 2142
    • (2000) Science , vol.288 , pp. 2141-2142
    • Lundblad, V.1
  • 8
    • 0032522443 scopus 로고    scopus 로고
    • The telomerase reverse transcriptase: Components and regulation
    • C.I. Nugent, and V. Lundblad The telomerase reverse transcriptase: components and regulation Genes Dev. 12 1998 1073 1085
    • (1998) Genes Dev. , vol.12 , pp. 1073-1085
    • Nugent, C.I.1    Lundblad, V.2
  • 9
    • 0029894237 scopus 로고    scopus 로고
    • Telomere length regulation
    • C.W. Greider Telomere length regulation Annu. Rev. Biochem. 65 1996 337 365
    • (1996) Annu. Rev. Biochem. , vol.65 , pp. 337-365
    • Greider, C.W.1
  • 11
    • 0028138773 scopus 로고
    • Solution structure of a specific DNA complex of the Myb DNA-binding domain with cooperative recognition helices
    • K. Ogata, S. Morikawa, H. Nakamura, A. Sekikawa, T. Inoue, H. Kanai, A. Sarai, S. Ishii, and Y. Nishimura Solution structure of a specific DNA complex of the Myb DNA-binding domain with cooperative recognition helices Cell 79 1994 639 648
    • (1994) Cell , vol.79 , pp. 639-648
    • Ogata, K.1    Morikawa, S.2    Nakamura, H.3    Sekikawa, A.4    Inoue, T.5    Kanai, H.6    Sarai, A.7    Ishii, S.8    Nishimura, Y.9
  • 12
    • 0027361377 scopus 로고
    • Recognition of specific DNA sequences by the c-myb protooncogene product: Role of three repeat units in the DNA-binding domain
    • J. Tanikawa, T. Yasukawa, M. Enari, K. Ogata, Y. Nishimura, S. Ishii, and A. Sarai Recognition of specific DNA sequences by the c-myb protooncogene product: role of three repeat units in the DNA-binding domain Proc. Natl. Acad. Sci. U.S.A. 90 1993 9320 9324
    • (1993) Proc. Natl. Acad. Sci. U.S.A. , vol.90 , pp. 9320-9324
    • Tanikawa, J.1    Yasukawa, T.2    Enari, M.3    Ogata, K.4    Nishimura, Y.5    Ishii, S.6    Sarai, A.7
  • 13
    • 0027105005 scopus 로고
    • Carboxy-terminal elements of c-Myb negatively regulate transcriptional activation in cis and in trans
    • J.W. Dubendorff, L.J. Whittaker, J.T. Eltman, and J.S. Lipsick Carboxy-terminal elements of c-Myb negatively regulate transcriptional activation in cis and in trans Genes Dev. 6 1992 2524 2535
    • (1992) Genes Dev. , vol.6 , pp. 2524-2535
    • Dubendorff, J.W.1    Whittaker, L.J.2    Eltman, J.T.3    Lipsick, J.S.4
  • 14
    • 0034604552 scopus 로고    scopus 로고
    • Sequence-specific DNA recognition by the Myb-like domain of plant telomeric protein RTBP1
    • E.Y. Yu, S.E. Kim, J.H. Kim, J.H. Ko, M.H. Cho, and I.K. Chung Sequence-specific DNA recognition by the Myb-like domain of plant telomeric protein RTBP1 J. Biol. Chem. 275 2000 24208 24214
    • (2000) J. Biol. Chem. , vol.275 , pp. 24208-24214
    • Yu, E.Y.1    Kim, S.E.2    Kim, J.H.3    Ko, J.H.4    Cho, M.H.5    Chung, I.K.6
  • 16
    • 0035844302 scopus 로고    scopus 로고
    • A plant gene encoding a Myb-like protein that binds telomeric GGTTAG repeats in vitro
    • C.M. Chen, C.T. Wang, and C.H. Ho A plant gene encoding a Myb-like protein that binds telomeric GGTTAG repeats in vitro J. Biol. Chem. 276 2001 16511 16519
    • (2001) J. Biol. Chem. , vol.276 , pp. 16511-16519
    • Chen, C.M.1    Wang, C.T.2    Ho, C.H.3
  • 17
    • 17444372705 scopus 로고    scopus 로고
    • AtTBP2 and AtTRP2 in Arabidopsis encode proteins that bind plant telomeric DNA and induce DNA bending in vitro
    • M.G. Hwang, K. Kim, W.K. Lee, and M.H. Cho AtTBP2 and AtTRP2 in Arabidopsis encode proteins that bind plant telomeric DNA and induce DNA bending in vitro Mol. Genet. Genomics 273 2005 66 75
    • (2005) Mol. Genet. Genomics , vol.273 , pp. 66-75
    • Hwang, M.G.1    Kim, K.2    Lee, W.K.3    Cho, M.H.4
  • 18
    • 0035839087 scopus 로고    scopus 로고
    • Sequence-specific binding property of Arabidopsis thaliana telomeric DNA binding protein 1 (AtTBP1)
    • M.G. Hwang, I.K. Chung, B.G. Kang, and M.H. Cho Sequence-specific binding property of Arabidopsis thaliana telomeric DNA binding protein 1 (AtTBP1) FEBS Lett. 503 2001 35 40
    • (2001) FEBS Lett. , vol.503 , pp. 35-40
    • Hwang, M.G.1    Chung, I.K.2    Kang, B.G.3    Cho, M.H.4
  • 19
    • 0031149554 scopus 로고    scopus 로고
    • PcMYB1, a novel plant protein containing a DNA-binding domain with one MYB repeat, interacts in vivo with a light-regulatory promoter unit
    • M. Feldbrugge, M. Sprenger, K. Hahlbrock, and B. Weisshaar PcMYB1, a novel plant protein containing a DNA-binding domain with one MYB repeat, interacts in vivo with a light-regulatory promoter unit Plant J. 11 1997 1079 1093
    • (1997) Plant J. , vol.11 , pp. 1079-1093
    • Feldbrugge, M.1    Sprenger, M.2    Hahlbrock, K.3    Weisshaar, B.4
  • 21
    • 84870515924 scopus 로고    scopus 로고
    • DNA-binding domain of AtTRB2 reveals unique features of a single Myb histone protein family that binds to both Arabidopsis- and human-type telomeric DNA sequences
    • W.K. Lee, J.H. Yun, W. Lee, and M.H. Cho DNA-binding domain of AtTRB2 reveals unique features of a single Myb histone protein family that binds to both Arabidopsis- and human-type telomeric DNA sequences Mol. Plant 5 2012 1406 1408
    • (2012) Mol. Plant , vol.5 , pp. 1406-1408
    • Lee, W.K.1    Yun, J.H.2    Lee, W.3    Cho, M.H.4
  • 22
    • 2542429720 scopus 로고    scopus 로고
    • Characterization of two Arabidopsis thaliana myb-like proteins showing affinity to telomeric DNA sequence
    • P. Schrumpfova, M. Kuchar, G. Mikova, L. Skrisovska, T. Kubicarova, and J. Fajkus Characterization of two Arabidopsis thaliana myb-like proteins showing affinity to telomeric DNA sequence Genome 47 2004 316 324
    • (2004) Genome , vol.47 , pp. 316-324
    • Schrumpfova, P.1    Kuchar, M.2    Mikova, G.3    Skrisovska, L.4    Kubicarova, T.5    Fajkus, J.6
  • 23
    • 12044259775 scopus 로고
    • Quantitative J correlation: A new approach for measuring homonuclear three bond J(HNHa) coupling constants in 15N-enriched proteins
    • G.W. Vuister, and A. Bax Quantitative J correlation: a new approach for measuring homonuclear three bond J(HNHa) coupling constants in 15N-enriched proteins J. Am. Chem. Soc. 115 1993 7772 7777
    • (1993) J. Am. Chem. Soc. , vol.115 , pp. 7772-7777
    • Vuister, G.W.1    Bax, A.2
  • 24
    • 44049117010 scopus 로고
    • Improved 3D triple-resonance NMR techniques applied to a 31-kDa protein
    • S. Grzesiek, and A. Bax Improved 3D triple-resonance NMR techniques applied to a 31-kDa protein J. Magn. Reson. 96 1992 432 440
    • (1992) J. Magn. Reson. , vol.96 , pp. 432-440
    • Grzesiek, S.1    Bax, A.2
  • 25
    • 0001689741 scopus 로고
    • Gradient-enhanced triple-resonance three-dimensional NMR experiments with improved sensitivity
    • D.R. Muhandiram, and L.E. Kay Gradient-enhanced triple-resonance three-dimensional NMR experiments with improved sensitivity J. Magn. Reson. 103 1994 203 216
    • (1994) J. Magn. Reson. , vol.103 , pp. 203-216
    • Muhandiram, D.R.1    Kay, L.E.2
  • 26
    • 0025341339 scopus 로고
    • 15N spectra of proteins: Heteronuclear triple-resonance three-dimensional NMR spectroscopy. Application to calmodulin
    • 15N spectra of proteins: heteronuclear triple-resonance three-dimensional NMR spectroscopy. Application to calmodulin Biochemistry 29 1990 4659 4667
    • (1990) Biochemistry , vol.29 , pp. 4659-4667
    • Ikura, M.1    Kay, L.E.2    Bax, A.3
  • 27
    • 0026951903 scopus 로고
    • Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions
    • M. Piotto, V. Saudek, and V. Sklenar Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions FEBS Lett. 2 1992 661 665
    • (1992) FEBS Lett. , vol.2 , pp. 661-665
    • Piotto, M.1    Saudek, V.2    Sklenar, V.3
  • 28
    • 44049118259 scopus 로고
    • Experiments for recording pure absorption heteronuclear correlation spectra using pulsed field gradients
    • A.L. Davis, J. Keeler, E.D. Laue, and D. Moskau Experiments for recording pure absorption heteronuclear correlation spectra using pulsed field gradients J. Magn. Reson. 98 1992 207 216
    • (1992) J. Magn. Reson. , vol.98 , pp. 207-216
    • Davis, A.L.1    Keeler, J.2    Laue, E.D.3    Moskau, D.4
  • 30
    • 0004040543 scopus 로고    scopus 로고
    • University of California San Francisco, CA
    • T.D. Goddard, and D.G. Kneller SPARKY 3 2004 University of California San Francisco, CA
    • (2004) SPARKY 3
    • Goddard, T.D.1    Kneller, D.G.2
  • 31
    • 0033003335 scopus 로고    scopus 로고
    • Protein backbone angle restraints from searching a database for chemical shift and sequence homology
    • G. Cornilescu, F. Delaglio, and A. Bax Protein backbone angle restraints from searching a database for chemical shift and sequence homology J. Biomol. NMR 13 1999 289 302
    • (1999) J. Biomol. NMR , vol.13 , pp. 289-302
    • Cornilescu, G.1    Delaglio, F.2    Bax, A.3
  • 32
    • 0036308102 scopus 로고    scopus 로고
    • Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA
    • T. Herrmann, P. Guntert, and K. Wuthrich Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA J. Mol. Biol. 319 2002 209 227
    • (2002) J. Mol. Biol. , vol.319 , pp. 209-227
    • Herrmann, T.1    Guntert, P.2    Wuthrich, K.3
  • 33
    • 0030339738 scopus 로고    scopus 로고
    • AQUA and PROCHECK-NMR: Programs for checking the quality of protein structures solved by NMR
    • R.A. Laskowski, J.A. Rullmannn, M.W. MacArthur, R. Kaptein, and J.M. Thornton AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR J. Biomol. NMR 8 1996 477 486
    • (1996) J. Biomol. NMR , vol.8 , pp. 477-486
    • Laskowski, R.A.1    Rullmannn, J.A.2    Macarthur, M.W.3    Kaptein, R.4    Thornton, J.M.5
  • 34
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • R. Koradi, M. Billeter, and K. Wuthrich MOLMOL: a program for display and analysis of macromolecular structures J. Mol. Graph. 14 51-55 1996 29 32
    • (1996) J. Mol. Graph. , vol.14 , Issue.5155 , pp. 29-32
    • Koradi, R.1    Billeter, M.2    Wuthrich, K.3
  • 37
    • 0028871926 scopus 로고
    • Dali: A network tool for protein structure comparison
    • L. Holm, and C. Sander Dali: a network tool for protein structure comparison Trends Biochem. Sci. 20 1995 478 480
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 478-480
    • Holm, L.1    Sander, C.2
  • 38
    • 0029934469 scopus 로고    scopus 로고
    • Alignment of three-dimensional protein structures: Network server for database searching
    • L. Holm, and C. Sander Alignment of three-dimensional protein structures: network server for database searching Methods Enzymol. 266 1996 653 662
    • (1996) Methods Enzymol. , vol.266 , pp. 653-662
    • Holm, L.1    Sander, C.2
  • 39
    • 30344457013 scopus 로고    scopus 로고
    • Solution structure of the Arabidopsis thaliana telomeric repeat-binding protein DNA binding domain: A new fold with an additional C-terminal helix
    • S.C. Sue, H.H. Hsiao, B.C. Chung, Y.H. Cheng, K.L. Hsueh, C.M. Chen, C.H. Ho, and T.H. Huang Solution structure of the Arabidopsis thaliana telomeric repeat-binding protein DNA binding domain: a new fold with an additional C-terminal helix J. Mol. Biol. 356 2006 72 85
    • (2006) J. Mol. Biol. , vol.356 , pp. 72-85
    • Sue, S.C.1    Hsiao, H.H.2    Chung, B.C.3    Cheng, Y.H.4    Hsueh, K.L.5    Chen, C.M.6    Ho, C.H.7    Huang, T.H.8
  • 40
    • 21444444520 scopus 로고    scopus 로고
    • How the human telomeric proteins TRF1 and TRF2 recognize telomeric DNA: A view from high-resolution crystal structures
    • R. Court, L. Chapman, L. Fairall, and D. Rhodes How the human telomeric proteins TRF1 and TRF2 recognize telomeric DNA: a view from high-resolution crystal structures EMBO Rep. 6 2005 39 45
    • (2005) EMBO Rep. , vol.6 , pp. 39-45
    • Court, R.1    Chapman, L.2    Fairall, L.3    Rhodes, D.4
  • 41
    • 11144223025 scopus 로고    scopus 로고
    • Comparison between TRF2 and TRF1 of their telomeric DNA-bound structures and DNA-binding activities
    • S. Hanaoka, A. Nagadoi, and Y. Nishimura Comparison between TRF2 and TRF1 of their telomeric DNA-bound structures and DNA-binding activities Protein Sci. 14 2005 119 130
    • (2005) Protein Sci. , vol.14 , pp. 119-130
    • Hanaoka, S.1    Nagadoi, A.2    Nishimura, Y.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.