메뉴 건너뛰기




Volumn 11, Issue 4, 2012, Pages

Probing the conformation of the ISWI ATPase domain with genetically encoded photoreactive crosslinkers and mass spectrometry

Author keywords

[No Author keywords available]

Indexed keywords

4 BENZOYL 4 PHENYLALANINE; ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATASE ISWI; AMINO ACID TRANSFER RNA LIGASE; HELICASE; PHENYLALANINE DERIVATIVE; TRANSFER RNA; UNCLASSIFIED DRUG; 4 BENZOYLPHENYLALANINE; 4-BENZOYLPHENYLALANINE; BENZOPHENONE DERIVATIVE; DROSOPHILA PROTEIN; DRUG DERIVATIVE; ISWI PROTEIN; PHENYLALANINE; TRANSCRIPTION FACTOR;

EID: 84859874809     PISSN: 15359476     EISSN: 15359484     Source Type: Journal    
DOI: 10.1074/mcp.M111.012088     Document Type: Article
Times cited : (45)

References (39)
  • 2
    • 0016864933 scopus 로고
    • Chemical Determination of Protein Neighborhoods in a Cellular Organelle
    • Lutter, L. C., and Kurland, C. G. (1975) Chemical Determination of Protein Neighborhoods in a Cellular Organelle. Mol. Cell. Biochem. 7, 105-116
    • (1975) Mol. Cell. Biochem. , vol.7 , pp. 105-116
    • Lutter, L.C.1    Kurland, C.G.2
  • 4
    • 79851513173 scopus 로고    scopus 로고
    • The beginning of a beautiful friendship: Cross-linking/mass spectrometry and modelling of proteins and multi-protein complexes
    • Rappsilber, J. (2011) The beginning of a beautiful friendship: cross-linking/mass spectrometry and modelling of proteins and multi-protein complexes. J. Struct. Biol. 173, 530-540
    • (2011) J. Struct. Biol. , vol.173 , pp. 530-540
    • Rappsilber, J.1
  • 5
    • 77950415030 scopus 로고    scopus 로고
    • Chemical cross-linking and mass spectrometry as a low-resolution protein structure determination technique
    • Singh, P., Panchaud, A., and Goodlett, D. R. (2010) Chemical cross-linking and mass spectrometry as a low-resolution protein structure determination technique. Anal. Chem. 82, 2636-2642
    • (2010) Anal. Chem. , vol.82 , pp. 2636-2642
    • Singh, P.1    Panchaud, A.2    Goodlett, D.R.3
  • 7
    • 78349301919 scopus 로고    scopus 로고
    • Computational modeling of laminin N-terminal domains using sparse distance constraints from disulfide bonds and chemical cross-linking
    • Kalkhof, S., Haehn, S., Paulsson, M., Smyth, N., Meiler, J., and Sinz, A. (2010) Computational modeling of laminin N-terminal domains using sparse distance constraints from disulfide bonds and chemical cross-linking. Proteins 78, 3409-3427
    • (2010) Proteins , vol.78 , pp. 3409-3427
    • Kalkhof, S.1    Haehn, S.2    Paulsson, M.3    Smyth, N.4    Meiler, J.5    Sinz, A.6
  • 11
    • 33747190864 scopus 로고    scopus 로고
    • Photoaffinity labeling combined with mass spectrometric approaches as a tool for structural proteomics
    • DOI 10.1586/14789450.3.4.399
    • Robinette, D., Neamati, N., Tomer, K. B., and Borchers, C. H. (2006) Photoaffinity labeling combined with mass spectrometric approaches as a tool for structural proteomics. Expert Rev. Proteomics 3, 399-408 (Pubitemid 44231983)
    • (2006) Expert Review of Proteomics , vol.3 , Issue.4 , pp. 399-408
    • Robinette, D.1    Neamati, N.2    Tomer, K.B.3    Borchers, C.H.4
  • 12
    • 0037021352 scopus 로고    scopus 로고
    • In vivo photocrosslinking with unnatural amino acid mutagenesis
    • DOI 10.1002/1439-7633(20021104)3:11<1135::AID-CBIC1135>3.0.CO;2-M
    • Chin, J. W., and Schultz, P. G. (2002) In vivo photocrosslinking with unnatural amino acid mutagenesis. Chembiochem. 3, 1135-1137 (Pubitemid 36008045)
    • (2002) ChemBioChem , vol.3 , Issue.11 , pp. 1135-1137
    • Chin, J.W.1    Schultz, P.G.2
  • 13
    • 18744396951 scopus 로고    scopus 로고
    • Protein photo-cross-linking in mammalian cells by site-specific incorporation of a photoreactive amino acid
    • DOI 10.1038/nmeth739
    • Hino, N., Okazaki, Y., Kobayashi, T., Hayashi, A., Sakamoto, K., and Yokoyama, S. (2005) Protein photo-cross-linking in mammalian cells by site-specific incorporation of a photoreactive amino acid. Nat. Methods 2, 201-206 (Pubitemid 41122127)
    • (2005) Nature Methods , vol.2 , Issue.3 , pp. 201-206
    • Hino, N.1    Okazaki, Y.2    Kobayashi, T.3    Hayashi, A.4    Sakamoto, K.5    Yokoyama, S.6
  • 14
    • 77956058146 scopus 로고    scopus 로고
    • Investigation of protein-protein interactions in living cells by chemical crosslinking and mass spectrometry
    • Sinz, A. (2010) Investigation of protein-protein interactions in living cells by chemical crosslinking and mass spectrometry. Anal. Bioanal. Chem. 397, 3433-3440
    • (2010) Anal. Bioanal. Chem. , vol.397 , pp. 3433-3440
    • Sinz, A.1
  • 15
    • 41449098104 scopus 로고    scopus 로고
    • Photoactivatable crosslinking sugars for capturing glycoprotein interactions
    • DOI 10.1021/ja7109772
    • Tanaka, Y., and Kohler, J. J. (2008) Photoactivatable crosslinking sugars for capturing glycoprotein interactions. J. Am. Chem. Soc. 130, 3278-3279 (Pubitemid 351456018)
    • (2008) Journal of the American Chemical Society , vol.130 , Issue.11 , pp. 3278-3279
    • Tanaka, Y.1    Kohler, J.J.2
  • 16
    • 77953167152 scopus 로고    scopus 로고
    • Revealing novel telomere proteins using in vivo cross-linking, tandem affinity purification, and label-free quantitative LC-FTICR-MS
    • Nittis, T., Guittat, L., LeDuc, R. D., Dao, B., Duxin, J. P., Rohrs, H., Townsend, R. R., and Stewart, S. A. (2010) Revealing novel telomere proteins using in vivo cross-linking, tandem affinity purification, and label-free quantitative LC-FTICR-MS. Mol. Cell. Proteomics 9, 1144-1156
    • (2010) Mol. Cell. Proteomics , vol.9 , pp. 1144-1156
    • Nittis, T.1    Guittat, L.2    LeDuc, R.D.3    Dao, B.4    Duxin, J.P.5    Rohrs, H.6    Townsend, R.R.7    Stewart, S.A.8
  • 18
    • 0028235205 scopus 로고
    • Benzophenone photophores in biochemistry
    • DOI 10.1021/bi00185a001
    • Dormán, G., and Prestwich, G. D. (1994) Benzophenone photophores in biochemistry. Biochemistry 33, 5661-5673 (Pubitemid 24184566)
    • (1994) Biochemistry , vol.33 , Issue.19 , pp. 5661-5673
    • Dorman, G.1    Prestwich, G.D.2
  • 19
    • 33745122231 scopus 로고    scopus 로고
    • Identification of multiple distinct Snf2 subfamilies with conserved structural motifs
    • DOI 10.1093/nar/gkl295
    • Flaus, A., Martin, D. M., Barton, G. J., and Owen-Hughes, T. (2006) Identification of multiple distinct Snf2 subfamilies with conserved structural motifs. Nucleic Acids Res. 34, 2887-2905 (Pubitemid 44540417)
    • (2006) Nucleic Acids Research , vol.34 , Issue.10 , pp. 2887-2905
    • Flaus, A.1    Martin, D.M.A.2    Barton, G.J.3    Owen-Hughes, T.4
  • 20
    • 18844457346 scopus 로고    scopus 로고
    • X-Ray structures of the sulfolobus solfataricus SWI2/SNF2 ATPase core and its complex with DNA
    • DOI 10.1016/j.cell.2005.03.026, PII S0092867405002989
    • Dürr, H., Körner, C., Müller, M., Hickmann, V., and Hopfner, K. P. (2005) X-ray structures of the Sulfolobus solfataricus SWI2/SNF2 ATPase core and its complex with DNA. Cell 121, 363-373 (Pubitemid 40692297)
    • (2005) Cell , vol.121 , Issue.3 , pp. 363-373
    • Durr, H.1    Korner, C.2    Muller, M.3    Hickmann, V.4    Hopfner, K.-P.5
  • 21
    • 77956522905 scopus 로고    scopus 로고
    • The chromodomains of the Chd1 chromatin remodeler regulate DNA access to the ATPase motor
    • Hauk, G., McKnight, J. N., Nodelman, I. M., and Bowman, G. D. (2010) The chromodomains of the Chd1 chromatin remodeler regulate DNA access to the ATPase motor. Mol. Cell 39, 711-723
    • (2010) Mol. Cell , vol.39 , pp. 711-723
    • Hauk, G.1    McKnight, J.N.2    Nodelman, I.M.3    Bowman, G.D.4
  • 23
    • 77953643054 scopus 로고    scopus 로고
    • Adding new chemistries to the genetic code
    • Liu, C. C., and Schultz, P. G. (2010) Adding new chemistries to the genetic code. Annu. Rev. Biochem. 79, 413-444
    • (2010) Annu. Rev. Biochem. , vol.79 , pp. 413-444
    • Liu, C.C.1    Schultz, P.G.2
  • 24
    • 0030026070 scopus 로고    scopus 로고
    • Femtomole sequencing of proteins from polyacrylamide gels by nano-electrospray mass spectrometry
    • Wilm, M., Shevchenko, A., Houthaeve, T., Breit, S., Schweigerer, L., Fotsis, T., and Mann, M. (1996) Femtomole sequencing of proteins from polyacrylamide gels by nano-electrospray mass spectrometry. Nature 379, 466-469
    • (1996) Nature , vol.379 , pp. 466-469
    • Wilm, M.1    Shevchenko, A.2    Houthaeve, T.3    Breit, S.4    Schweigerer, L.5    Fotsis, T.6    Mann, M.7
  • 26
    • 33646264529 scopus 로고    scopus 로고
    • Advances in proteomics data analysis and display using an accurate mass and time tag approach
    • Zimmer, J. S., Monroe, M. E., Qian, W. J., and Smith, R. D. (2006) Advances in proteomics data analysis and display using an accurate mass and time tag approach. Mass Spectrom. Rev. 25, 450-482
    • (2006) Mass Spectrom. Rev. , vol.25 , pp. 450-482
    • Zimmer, J.S.1    Monroe, M.E.2    Qian, W.J.3    Smith, R.D.4
  • 27
    • 4544370533 scopus 로고    scopus 로고
    • Improved peptide identification in proteomics by two consecutive stages of mass spectrometric fragmentation
    • DOI 10.1073/pnas.0405549101
    • Olsen, J. V., and Mann, M. (2004) Improved peptide identification in proteomics by two consecutive stages of mass spectrometric fragmentation. Proc. Natl. Acad. Sci. U.S.A. 101, 13417-13422 (Pubitemid 39238417)
    • (2004) Proceedings of the National Academy of Sciences of the United States of America , vol.101 , Issue.37 , pp. 13417-13422
    • Olsen, J.V.1    Mann, M.2
  • 28
    • 0027136282 scopus 로고
    • Comparative protein modelling by satisfaction of spatial restraints
    • DOI 10.1006/jmbi.1993.1626
    • Sali, A., and Blundell, T. L. (1993) Comparative protein modelling by satisfaction of spatial restraints. J. Mol. Biol. 234, 779-815 (Pubitemid 24007801)
    • (1993) Journal of Molecular Biology , vol.234 , Issue.3 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 29
    • 33747743113 scopus 로고    scopus 로고
    • Interdomain communication in DNA topoisomerase II: DNA binding and enzyme activation
    • DOI 10.1074/jbc.M604119200
    • Mueller-Planitz, F., and Herschlag, D. (2006) Interdomain communication in DNA topoisomerase II. DNA binding and enzyme activation. J. Biol. Chem. 281, 23395-23404 (Pubitemid 44274114)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.33 , pp. 23395-23404
    • Mueller-Planitz, F.1    Herschlag, D.2
  • 30
    • 0033289822 scopus 로고    scopus 로고
    • Expression and purification of recombinant histones and nucleosome reconstitution
    • Luger, K., Rechsteiner, T. J., and Richmond, T. J. (1999) Expression and purification of recombinant histones and nucleosome reconstitution. Methods Mol. Biol. 119, 1-16
    • (1999) Methods Mol. Biol. , vol.119 , pp. 1-16
    • Luger, K.1    Rechsteiner, T.J.2    Richmond, T.J.3
  • 31
    • 67650725820 scopus 로고    scopus 로고
    • The biology of chromatin remodeling complexes
    • Clapier, C. R., and Cairns, B. R. (2009) The biology of chromatin remodeling complexes. Annu. Rev. Biochem. 78, 273-304
    • (2009) Annu. Rev. Biochem. , vol.78 , pp. 273-304
    • Clapier, C.R.1    Cairns, B.R.2
  • 32
    • 79952468153 scopus 로고    scopus 로고
    • SnapShot: Chromatin remodeling: ISWI
    • Yadon, A. N., and Tsukiyama, T. (2011) SnapShot: Chromatin remodeling: ISWI. Cell 144, 453-453 e451
    • (2011) Cell , vol.144
    • Yadon, A.N.1    Tsukiyama, T.2
  • 33
    • 11144357573 scopus 로고    scopus 로고
    • Characterization of the Binding Site for Inhibitors of the HPV11 E1-E2 Protein Interaction on the E2 Transactivation Domain by Photoaffinity Labeling and Mass Spectrometry
    • DOI 10.1021/ac035335o
    • Davidson, W., McGibbon, G. A., White, P. W., Yoakim, C., Hopkins, J. L., Guse, I., Hambly, D. M., Frego, L., Ogilvie, W. W., Lavallée, P., and Archambault, J. (2004) Characterization of the binding site for inhibitors of the HPV11 E1-E2 protein interaction on the E2 Transactivation domain by photoaffinity labeling and mass spectrometry. Anal. Chem. 76, 2095-2102 (Pubitemid 38451531)
    • (2004) Analytical Chemistry , vol.76 , Issue.7 , pp. 2095-2102
    • Davidson, W.1    McGibbon, G.A.2    White, P.W.3    Yoakim, C.4    Hopkins, J.L.5    Guse, I.6    Hambly, D.M.7    Frego, L.8    Ogilvie, W.W.9    Lavallee, P.10    Archambault, J.11
  • 35
    • 67549115599 scopus 로고    scopus 로고
    • Exploring the interactions between signal sequences and E. coli SRP by two distinct and complementary crosslinking methods
    • Clérico, E. M., Szymanska, A., and Gierasch, L. M. (2009) Exploring the interactions between signal sequences and E. coli SRP by two distinct and complementary crosslinking methods. Biopolymers 92, 201-211
    • (2009) Biopolymers , vol.92 , pp. 201-211
    • Clérico, E.M.1    Szymanska, A.2    Gierasch, L.M.3
  • 36
    • 0032575523 scopus 로고    scopus 로고
    • Parathyroid hormone-receptor interactions identified directly by photocross-linking and molecular modeling studies
    • DOI 10.1074/jbc.273.35.22498
    • Bisello, A., Adams, A. E., Mierke, D. F., Pellegrini, M., Rosenblatt, M., Suva, L. J., and Chorev, M. (1998) Parathyroid hormone-receptor interactions identified directly by photocross-linking and molecular modeling studies. J. Biol. Chem. 273, 22498-22505 (Pubitemid 28399816)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.35 , pp. 22498-22505
    • Bisello, A.1    Adams, A.E.2    Mierke, D.F.3    Pellegrini, M.4    Rosenblatt, M.5    Suva, L.J.6    Chorev, M.7
  • 37
    • 69249137421 scopus 로고    scopus 로고
    • Heterobifunctional isotope-labeled amine-reactive photo-cross-linker for structural investigation of proteins by matrix-assisted laser desorption/ionization tandem time-of-flight and electrospray ionization LTQ-Orbitrap mass spectrometry
    • Krauth, F., Ihling, C. H., Rüttinger, H. H., and Sinz, A. (2009) Heterobifunctional isotope-labeled amine-reactive photo-cross-linker for structural investigation of proteins by matrix-assisted laser desorption/ionization tandem time-of-flight and electrospray ionization LTQ-Orbitrap mass spectrometry. Rapid Commun. Mass Spectrom. 23, 2811-2818
    • (2009) Rapid Commun. Mass Spectrom. , vol.23 , pp. 2811-2818
    • Krauth, F.1    Ihling, C.H.2    Rüttinger, H.H.3    Sinz, A.4
  • 38
    • 33644886015 scopus 로고    scopus 로고
    • Methionine acts as a "magnet" in photoaffinity crosslinking experiments
    • Wittelsberger, A., Thomas, B. E., Mierke, D. F., and Rosenblatt, M. (2006) Methionine acts as a "magnet" in photoaffinity crosslinking experiments. FEBS Lett. 580, 1872-1876
    • (2006) FEBS Lett. , vol.580 , pp. 1872-1876
    • Wittelsberger, A.1    Thomas, B.E.2    Mierke, D.F.3    Rosenblatt, M.4
  • 39
    • 47749144375 scopus 로고    scopus 로고
    • Chances and pitfalls of chemical crosslinking with amine-reactive N-hydroxysuccinimide esters
    • Kalkhof, S., and Sinz, A. (2008) Chances and pitfalls of chemical crosslinking with amine-reactive N-hydroxysuccinimide esters. Anal. Bioanal. Chem. 392, 305-312
    • (2008) Anal. Bioanal. Chem. , vol.392 , pp. 305-312
    • Kalkhof, S.1    Sinz, A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.