메뉴 건너뛰기




Volumn 9, Issue 6, 2010, Pages 1144-1156

Revealing novel telomere proteins using in vivo cross-linking, tandem affinity purification, and label-free quantitative LC-FTICR-MS

Author keywords

[No Author keywords available]

Indexed keywords

BINDING PROTEIN; DNA; EPITOPE; METALLOPROTEINASE; NANOPARTICLE;

EID: 77953167152     PISSN: 15359476     EISSN: None     Source Type: Journal    
DOI: 10.1074/mcp.M900490-MCP200     Document Type: Article
Times cited : (47)

References (51)
  • 2
    • 0037337310 scopus 로고    scopus 로고
    • A proteomics strategy to elucidate functional protein-protein interactions applied to EGF signaling
    • DOI 10.1038/nbt790
    • Blagoev, B., Kratchmarova, I., Ong, S. E., Nielsen, M., Foster, L. J., and Mann, M. (2003) A proteomics strategy to elucidate functional protein-protein interactions applied to EGF signaling. Nat. Biotechnol. 21, 315-318 (Pubitemid 36314817)
    • (2003) Nature Biotechnology , vol.21 , Issue.3 , pp. 315-318
    • Blagoev, B.1    Kratchmarova, I.2    Ong, S.-E.3    Nielsen, M.4    Foster, L.J.5    Mann, M.6
  • 4
    • 13244260803 scopus 로고    scopus 로고
    • A novel strategy for quantitative proteomics using isotope-coded protein labels
    • DOI 10.1002/pmic.200400873
    • Schmidt, A., Kellermann, J., and Lottspeich, F. (2005) A novel strategy for quantitative proteomics using isotope-coded protein labels. Proteomics 5, 4-15 (Pubitemid 40189632)
    • (2005) Proteomics , vol.5 , Issue.1 , pp. 4-15
    • Schmidt, A.1    Kellermann, J.2    Lottspeich, F.3
  • 5
    • 0036583926 scopus 로고    scopus 로고
    • Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics
    • Ong, S. E., Blagoev, B., Kratchmarova, I., Kristensen, D. B., Steen, H., Pandey, A., and Mann, M. (2002) Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics. Mol. Cell. Proteomics 1, 376-386
    • (2002) Mol. Cell. Proteomics , vol.1 , pp. 376-386
    • Ong, S.E.1    Blagoev, B.2    Kratchmarova, I.3    Kristensen, D.B.4    Steen, H.5    Pandey, A.6    Mann, M.7
  • 6
    • 1342282907 scopus 로고    scopus 로고
    • Quantitative proteomic identification of six4 as the trex-binding factor in the muscle creatine kinase enhancer
    • Himeda, C. L., Ranish, J. A., Angello, J. C., Maire, P., Aebersold, R., and Hauschka, S. D. (2004) Quantitative proteomic identification of six4 as the trex-binding factor in the muscle creatine kinase enhancer. Mol. Cell. Biol. 24, 2132-2143
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 2132-2143
    • Himeda, C.L.1    Ranish, J.A.2    Angello, J.C.3    Maire, P.4    Aebersold, R.5    Hauschka, S.D.6
  • 7
    • 33947182552 scopus 로고    scopus 로고
    • An integrated mass spectrometric and computational framework for the analysis of protein interaction networks
    • Rinner, O., Mueller, L. N., HubáleḱM., Müller, M., Gstaiger, M., and Aebersold, R. (2007) An integrated mass spectrometric and computational framework for the analysis of protein interaction networks. Nat. Biotechnol. 25, 345-352
    • (2007) Nat. Biotechnol. , vol.25 , pp. 345-352
    • Rinner, O.1    Mueller, L.N.2    HubáleḱM3    Müller, M.4    Gstaiger, M.5    Aebersold, R.6
  • 8
    • 24944460598 scopus 로고    scopus 로고
    • Shelterin: The protein complex that shapes and safeguards human telomeres
    • de Lange, T. (2005) Shelterin: the protein complex that shapes and safeguards human telomeres. Genes Dev. 19, 2100-2110
    • (2005) Genes Dev. , vol.19 , pp. 2100-2110
    • De Lange, T.1
  • 9
    • 10944240539 scopus 로고    scopus 로고
    • Telosome, a mammalian telomere-associated complex formed by multiple telomeric proteins
    • Liu, D., O'Connor, M. S., Qin, J., and Songyang, Z. (2004) Telosome, a mammalian telomere-associated complex formed by multiple telomeric proteins. J. Biol. Chem. 279, 51338-51342
    • (2004) J. Biol. Chem. , vol.279 , pp. 51338-51342
    • Liu, D.1    O'Connor, M.S.2    Qin, J.3    Songyang, Z.4
  • 10
    • 0035929353 scopus 로고    scopus 로고
    • Switching and signaling at the telomere
    • Blackburn, E. H. (2001) Switching and signaling at the telomere. Cell 106, 661-673
    • (2001) Cell , vol.106 , pp. 661-673
    • Blackburn, E.H.1
  • 11
    • 1642523697 scopus 로고    scopus 로고
    • Indecent exposure: When telomeres become uncapped
    • Ferreira, M. G., Miller, K. M., and Cooper, J. P. (2004) Indecent exposure: when telomeres become uncapped. Mol. Cell 13, 7-18
    • (2004) Mol. Cell , vol.13 , pp. 7-18
    • Ferreira, M.G.1    Miller, K.M.2    Cooper, J.P.3
  • 12
    • 0042420304 scopus 로고    scopus 로고
    • DNA damage foci at dysfunctional telomeres
    • Takai, H., Smogorzewska, A., and de Lange, T. (2003) DNA damage foci at dysfunctional telomeres. Curr. Biol. 13, 1549-1556
    • (2003) Curr. Biol. , vol.13 , pp. 1549-1556
    • Takai, H.1    Smogorzewska, A.2    De Lange, T.3
  • 14
    • 0347416975 scopus 로고    scopus 로고
    • ERCC1/XPF Removes the 3′ Overhang from Uncapped Telomeres and Represses Formation of Telomeric DNA-Containing Double Minute Chromosomes
    • DOI 10.1016/S1097-2765(03)00478-7
    • Zhu, X. D., Niedernhofer, L., Kuster, B., Mann, M., Hoeijmakers, J. H., and de Lange, T. (2003) ERCC1/XPF removes the 3′ overhang from uncapped telomeres and represses formation of telomeric DNA-containing double minute chromosomes. Mol. Cell 12, 1489-1498 (Pubitemid 38037017)
    • (2003) Molecular Cell , vol.12 , Issue.6 , pp. 1489-1498
    • Zhu, X.-D.1    Niedernhofer, L.2    Kuster, B.3    Mann, M.4    Hoeijmakers, J.H.J.5    De Lange, T.6
  • 16
    • 0033568014 scopus 로고    scopus 로고
    • Normal human telomeres are not late replicating
    • Wright, W. E., Tesmer, V. M., Liao, M. L., and Shay, J. W. (1999) Normal human telomeres are not late replicating. Exp. Cell Res. 251, 492-499
    • (1999) Exp. Cell Res. , vol.251 , pp. 492-499
    • Wright, W.E.1    Tesmer, V.M.2    Liao, M.L.3    Shay, J.W.4
  • 17
    • 0037326054 scopus 로고    scopus 로고
    • Telomeric protein distributions and remodeling through the cell cycle in Saccharomyces cerevisiae
    • DOI 10.1091/mbc.E02-08-0457
    • Smith, C. D., Smith, D. L., DeRisi, J. L., and Blackburn, E. H. (2003) Telomeric protein distributions and remodeling through the cell cycle in Saccharomyces cerevisiae. Mol. Biol. Cell 14, 556-570 (Pubitemid 36237016)
    • (2003) Molecular Biology of the Cell , vol.14 , Issue.2 , pp. 556-570
    • Smith, C.D.1    Smith, D.L.2    Derisi, J.L.3    Blackburn, E.H.4
  • 18
    • 10344256183 scopus 로고    scopus 로고
    • Defective telomere lagging strand synthesis in cells lacking WRN helicase activity
    • DOI 10.1126/science.1103619
    • Crabbe, L., Verdun, R. E., Haggblom, C. I., and Karlseder, J. (2004) Defective telomere lagging strand synthesis in cells lacking WRN helicase activity. Science 306, 1951-1953 (Pubitemid 39627862)
    • (2004) Science , vol.306 , Issue.5703 , pp. 1951-1953
    • Crabbe, L.1    Verdun, R.E.2    Haggblom, C.I.3    Karlseder, J.4
  • 19
    • 0038451396 scopus 로고    scopus 로고
    • POT1 as a terminal transducer of TRF-1 telomere length control
    • Loayza, D., and De Lange, T. (2003) POT1 as a terminal transducer of TRF-1 telomere length control. Nature 423, 1013-1018
    • (2003) Nature , vol.423 , pp. 1013-1018
    • Loayza, D.1    De Lange, T.2
  • 20
    • 0031040702 scopus 로고    scopus 로고
    • Intracellular assembly and degradation of apolipoprotein B-100- Containing lipoproteins in digitonin-permeabilized HEP G2 cells
    • DOI 10.1074/jbc.272.8.5031
    • Adeli, K., Wettesten, M., Asp, L., Mohammadi, A., Macri, J., and Olofsson, S. O. (1997) Intracellular assembly and degradation of apolipoprotein B-100-containing lipoproteins in digitonin-permeabilized HEP G2 cells. J. Biol. Chem. 272, 5031-5039 (Pubitemid 27090056)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.8 , pp. 5031-5039
    • Adeli, K.1    Wettesten, M.2    Asp, L.3    Mohammadi, A.4    Macri, J.5    Olofsson, S.-O.6
  • 21
    • 0347381286 scopus 로고    scopus 로고
    • Immunoaffinity purification of mammalian protein complexes
    • Nakatani, Y., and Ogryzko, V. (2003) Immunoaffinity purification of mammalian protein complexes. Methods Enzymol. 370, 430-444
    • (2003) Methods Enzymol. , vol.370 , pp. 430-444
    • Nakatani, Y.1    Ogryzko, V.2
  • 22
    • 55249104730 scopus 로고    scopus 로고
    • Sample preparation and in-solution protease digestion of proteins for chromatography-based proteomic analysis
    • Chapter 23, Unit
    • Washburn, M. P. (2008) Sample preparation and in-solution protease digestion of proteins for chromatography-based proteomic analysis. Curr. Protoc. Protein Sci. Chapter 23, Unit 23.6.1-23.6.11
    • (2008) Curr. Protoc. Protein Sci.
    • Washburn, M.P.1
  • 23
    • 0035870165 scopus 로고    scopus 로고
    • Matrix-assisted laser desorption/ ionization coupled with quadrupole/orthogonal acceleration time-offlight mass spectrometry for protein discovery, identification, and structural analysis
    • Baldwin, M. A., Medzihradszky, K. F., Lock, C. M., Fisher, B., Settineri, T. A., and Burlingame, A. L. (2001) Matrix-assisted laser desorption/ ionization coupled with quadrupole/orthogonal acceleration time-offlight mass spectrometry for protein discovery, identification, and structural analysis. Anal. Chem. 73, 1707-1720
    • (2001) Anal. Chem. , vol.73 , pp. 1707-1720
    • Baldwin, M.A.1    Medzihradszky, K.F.2    Lock, C.M.3    Fisher, B.4    Settineri, T.A.5    Burlingame, A.L.6
  • 24
    • 49849105549 scopus 로고    scopus 로고
    • Label-free detection of differential protein expression by LC/MALDI mass spectrometry
    • Neubert, H., Bonnert, T. P., Rumpel, K., Hunt, B. T., Henle, E. S., and James, I. T. (2008) Label-free detection of differential protein expression by LC/MALDI mass spectrometry. J. Proteome Res. 7, 2270-2279
    • (2008) J. Proteome Res. , vol.7 , pp. 2270-2279
    • Neubert, H.1    Bonnert, T.P.2    Rumpel, K.3    Hunt, B.T.4    Henle, E.S.5    James, I.T.6
  • 25
    • 3142679378 scopus 로고    scopus 로고
    • POT1-interacting protein PIP1: A telomere length regulator that recruits POT1 to the TIN2/TRF1 complex
    • Ye, J. Z., Hockemeyer, D., Krutchinsky, A. N., Loayza, D., Hooper, S. M., Chait, B. T., and de Lange, T. (2004) POT1-interacting protein PIP1: a telomere length regulator that recruits POT1 to the TIN2/TRF1 complex. Genes Dev. 18, 1649-1654
    • (2004) Genes Dev. , vol.18 , pp. 1649-1654
    • Ye, J.Z.1    Hockemeyer, D.2    Krutchinsky, A.N.3    Loayza, D.4    Hooper, S.M.5    Chait, B.T.6    De Lange, T.7
  • 26
    • 33747051742 scopus 로고    scopus 로고
    • A critical role for TPP1 and TIN2 interaction in high-order telomeric complex assembly
    • O'Connor, M. S., Safari, A., Xin, H., Liu, D., and Songyang, Z. (2006) A critical role for TPP1 and TIN2 interaction in high-order telomeric complex assembly. Proc. Natl. Acad. Sci. U.S.A. 103, 11874-11879
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 11874-11879
    • O'Connor, M.S.1    Safari, A.2    Xin, H.3    Liu, D.4    Songyang, Z.5
  • 27
    • 10644254712 scopus 로고    scopus 로고
    • Identification of protein-protein interactions using in vivo cross-linking and mass spectrometry
    • DOI 10.1002/pmic.200400856
    • Vasilescu, J., Guo, X., and Kast, J. (2004) Identification of protein-protein interactions using in vivo cross-linking and mass spectrometry. Proteomics 4, 3845-3854 (Pubitemid 39657461)
    • (2004) Proteomics , vol.4 , Issue.12 , pp. 3845-3854
    • Vasilescu, J.1    Guo, X.2    Kast, J.3
  • 28
    • 0034716904 scopus 로고    scopus 로고
    • Identification of human Rap1: Implications for telomere evolution
    • Li, B., Oestreich, S., and de Lange, T. (2000) Identification of human Rap1: implications for telomere evolution. Cell 101, 471-483
    • (2000) Cell , vol.101 , pp. 471-483
    • Li, B.1    Oestreich, S.2    De Lange, T.3
  • 29
    • 10744223820 scopus 로고    scopus 로고
    • Metz, B., Kersten, G. F., Hoogerhout, P., Brugghe, H. F., Timmermans, H. A., de Jong, A., Meiring, H., ten Hove, J., Hennink, W. E., Crommelin, D. J., and Jiskoot, W. (2004) Identification of formaldehyde-induced modifications in proteins: reactions with model peptides. J. Biol. Chem. 279, 6235-6243
    • Metz, B.1    Kersten, G.F.2
  • 30
    • 0017075525 scopus 로고
    • Chemical probes of extended biological structures: Synthesis and properties of the cleavable protein cross-linking reagent [35S] dithiobis(succinimidyl propionate)
    • Lomant, A. J., and Fairbanks, G. (1976) Chemical probes of extended biological structures: synthesis and properties of the cleavable protein cross-linking reagent [35S]dithiobis(succinimidyl propionate). J. Mol. Biol. 104, 243-261
    • (1976) J. Mol. Biol. , vol.104 , pp. 243-261
    • Lomant, A.J.1    Fairbanks, G.2
  • 31
    • 0038373278 scopus 로고    scopus 로고
    • The spatial organization of apolipoprotein A-I on the edge of discoidal high density lipoprotein particles: A mass spectrometry study
    • Davidson, W. S., and Hilliard, G. M. (2003) The spatial organization of apolipoprotein A-I on the edge of discoidal high density lipoprotein particles: a mass spectrometry study. J. Biol. Chem. 278, 27199-27207
    • (2003) J. Biol. Chem. , vol.278 , pp. 27199-27207
    • Davidson, W.S.1    Hilliard, G.M.2
  • 32
    • 33846570438 scopus 로고    scopus 로고
    • A proteomics approach for identifying osmotic-stress-related proteins in rice
    • DOI 10.1016/j.phytochem.2006.11.005, PII S0031942206006960
    • Zang, X., and Komatsu, S. (2007) A proteomics approach for identifying osmotic-stress-related proteins in rice. Phytochemistry 68, 426-437 (Pubitemid 46186438)
    • (2007) Phytochemistry , vol.68 , Issue.4 , pp. 426-437
    • Zang, X.1    Komatsu, S.2
  • 33
    • 29944434644 scopus 로고    scopus 로고
    • Multifactorial contributions to an acute DNA damage response by BRCA1/BARD1-containing complexes
    • DOI 10.1101/gad.1381306
    • Greenberg, R. A., Sobhian, B., Pathania, S., Cantor, S. B., Nakatani, Y., and Livingston, D. M. (2006) Multifactorial contributions to an acute DNA damage response by BRCA1/BARD1-containing complexes. Genes Dev. 20, 34-46 (Pubitemid 43042666)
    • (2006) Genes and Development , vol.20 , Issue.1 , pp. 34-46
    • Greenberg, R.A.1    Sobhian, B.2    Pathania, S.3    Cantor, S.B.4    Nakatani, Y.5    Livingston, D.M.6
  • 34
    • 40549107755 scopus 로고    scopus 로고
    • Comparative LC-MS: A landscape of peaks and valleys
    • America, A. H., and Cordewener, J. H. (2008) Comparative LC-MS: a landscape of peaks and valleys. Proteomics 8, 731-749
    • (2008) Proteomics , vol.8 , pp. 731-749
    • America, A.H.1    Cordewener, J.H.2
  • 37
    • 0027263365 scopus 로고
    • Nuclear proteins that bind the pre-mRNA 3' splice site sequence r(UUAG/G) and the human telomeric DNA sequence d(TTAGGG)(n)
    • Ishikawa, F., Matunis, M. J., Dreyfuss, G., and Cech, T. R. (1993) Nuclear proteins that bind the pre-mRNA 3′ splice site sequence r(UUAG/G) and the human telomeric DNA sequence d(TTAGGG)n. Mol. Cell. Biol. 13, 4301-4310 (Pubitemid 23187659)
    • (1993) Molecular and Cellular Biology , vol.13 , Issue.7 , pp. 4301-4310
    • Ishikawa, F.1    Matunis, M.J.2    Dreyfuss, G.3    Cech, T.R.4
  • 39
    • 0031800617 scopus 로고    scopus 로고
    • Telomere elongation by hnRNP A1 and a derivative that interacts with telomeric repeats and telomerase
    • LaBranche, H., Dupuis, S., Ben-David, Y., Bani, M. R., Wellinger, R. J., and Chabot, B. (1998) Telomere elongation by hnRNP A1 and a derivative that interacts with telomeric repeats and telomerase. Nat. Genet. 19, 199-202
    • (1998) Nat. Genet. , vol.19 , pp. 199-202
    • Labranche, H.1    Dupuis, S.2    Ben-David, Y.3    Bani, M.R.4    Wellinger, R.J.5    Chabot, B.6
  • 40
    • 0034462197 scopus 로고    scopus 로고
    • Heterogeneous nuclear ribonucleoproteins C1 and C2 associate with the RNA component of human telomerase
    • Ford, L. P., Suh, J. M., Wright, W. E., and Shay, J. W. (2000) Heterogeneous nuclear ribonucleoproteins C1 and C2 associate with the RNA component of human telomerase. Mol. Cell. Biol. 20, 9084-9091
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 9084-9091
    • Ford, L.P.1    Suh, J.M.2    Wright, W.E.3    Shay, J.W.4
  • 41
    • 0033927902 scopus 로고    scopus 로고
    • In vitro properties of the conserved mammalian protein hnRNP D suggest a role in telomere maintenance
    • Eversole, A., and Maizels, N. (2000) In vitro properties of the conserved mammalian protein hnRNP D suggest a role in telomere maintenance. Mol. Cell. Biol. 20, 5425-5432
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 5425-5432
    • Eversole, A.1    Maizels, N.2
  • 43
    • 0035844136 scopus 로고    scopus 로고
    • Stable association of hsp90 and p23, but Not hsp70, with active human telomerase
    • Forsythe, H. L., Jarvis, J. L., Turner, J. W., Elmore, L. W., and Holt, S. E. (2001) Stable association of hsp90 and p23, but Not hsp70, with active human telomerase. J. Biol. Chem. 276, 15571-15574
    • (2001) J. Biol. Chem. , vol.276 , pp. 15571-15574
    • Forsythe, H.L.1    Jarvis, J.L.2    Turner, J.W.3    Elmore, L.W.4    Holt, S.E.5
  • 45
    • 37349043972 scopus 로고    scopus 로고
    • Telomeric repeat containing RNA and RNA surveillance factors at mammalian chromosome ends
    • Azzalin, C. M., Reichenbach, P., Khoriauli, L., Giulotto, E., and Lingner, J. (2007) Telomeric repeat containing RNA and RNA surveillance factors at mammalian chromosome ends. Science 318, 798-801
    • (2007) Science , vol.318 , pp. 798-801
    • Azzalin, C.M.1    Reichenbach, P.2    Khoriauli, L.3    Giulotto, E.4    Lingner, J.5
  • 46
    • 0026668731 scopus 로고
    • A mammalian factor that binds telomeric TTAGGG repeats in vitro
    • Zhong, Z., Shiue, L., Kaplan, S., and de Lange, T. (1992) A mammalian factor that binds telomeric TTAGGG repeats in vitro. Mol. Cell. Biol. 12, 4834-4843
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 4834-4843
    • Zhong, Z.1    Shiue, L.2    Kaplan, S.3    De Lange, T.4
  • 48
    • 33745652501 scopus 로고    scopus 로고
    • Apollo, an Artemis-related nuclease, interacts with TRF2 and protects human telomeres in S phase
    • van Overbeek, M., and de Lange, T. (2006) Apollo, an Artemis-related nuclease, interacts with TRF2 and protects human telomeres in S phase. Curr. Biol. 16, 1295-1302
    • (2006) Curr. Biol. , vol.16 , pp. 1295-1302
    • Van Overbeek, M.1    De Lange, T.2
  • 49
    • 33645703441 scopus 로고    scopus 로고
    • A tandem affinity tag for two-step purification under fully denaturing conditions: Application in ubiquitin profiling and protein complex identification combined with in vivo cross-linking
    • Tagwerker, C., Flick, K., Cui, M., Guerrero, C., Dou, Y., Auer, B., Baldi, P., Huang, L., and Kaiser, P. (2006) A tandem affinity tag for two-step purification under fully denaturing conditions: application in ubiquitin profiling and protein complex identification combined with in vivo cross-linking. Mol. Cell. Proteomics 5, 737-748
    • (2006) Mol. Cell. Proteomics , vol.5 , pp. 737-748
    • Tagwerker, C.1    Flick, K.2    Cui, M.3    Guerrero, C.4    Dou, Y.5    Auer, B.6    Baldi, P.7    Huang, L.8    Kaiser, P.9
  • 50
    • 4444230597 scopus 로고    scopus 로고
    • Nucleolar localization of the human telomeric repeat binding factor 2 (TRF2)
    • Zhang, S., Hemmerich, P., and Grosse, F. (2004) Nucleolar localization of the human telomeric repeat binding factor 2 (TRF2). J. Cell Sci. 117, 3935-3945
    • (2004) J. Cell Sci. , vol.117 , pp. 3935-3945
    • Zhang, S.1    Hemmerich, P.2    Grosse, F.3
  • 51
    • 58149085861 scopus 로고    scopus 로고
    • Purification of proteins associated with specific genomic loci
    • Déjardin, J., and Kingston, R. E. (2009) Purification of proteins associated with specific genomic loci. Cell 136, 175-186
    • (2009) Cell , vol.136 , pp. 175-186
    • Déjardin, J.1    Kingston, R.E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.