메뉴 건너뛰기




Volumn 396, Issue 3, 2010, Pages 732-746

Increase in Backbone Mobility of the VTS1p-SAM Domain on Binding to SRE-RNA

Author keywords

NMR; Protein RNA interaction; SRE RNA; VTS1p SAM domain

Indexed keywords

PROTEIN; PURINE; PYRIMIDINE; SMAUG RECOGNITION ELEMENT RIBONUCLEIC ACID; UNCLASSIFIED DRUG; VTS1P STERILE ALPHA MOTIF; FUNGAL RNA; RNA BINDING PROTEIN; SACCHAROMYCES CEREVISIAE PROTEIN; VTS1 PROTEIN, S CEREVISIAE;

EID: 77949325480     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2009.12.004     Document Type: Article
Times cited : (23)

References (48)
  • 2
    • 0042320368 scopus 로고    scopus 로고
    • SAM breaks its stereotype
    • Hall T.M.T. SAM breaks its stereotype. Nat. Struct. Biol. 2003, 10:677-679.
    • (2003) Nat. Struct. Biol. , vol.10 , pp. 677-679
    • Hall, T.M.T.1
  • 3
    • 0042490664 scopus 로고    scopus 로고
    • The RNA-binding SAM domain of Smaug defines a new family of post-transcriptional regulators
    • Aviv T., Lin Z., Lau S., Rendl L.M., Sicheri F., Smibert C.A. The RNA-binding SAM domain of Smaug defines a new family of post-transcriptional regulators. Nat. Struct. Biol. 2003, 10:614-621.
    • (2003) Nat. Struct. Biol. , vol.10 , pp. 614-621
    • Aviv, T.1    Lin, Z.2    Lau, S.3    Rendl, L.M.4    Sicheri, F.5    Smibert, C.A.6
  • 4
    • 0029958353 scopus 로고    scopus 로고
    • Smaug protein represses translation of unlocalized nanos mRNA in the Drosophila embryo
    • Smibert C.A., Wilson J.E., Kerr K., Macdonald P.M. smaug protein represses translation of unlocalized nanos mRNA in the Drosophila embryo. Genes Dev. 1996, 10:2600-2609.
    • (1996) Genes Dev. , vol.10 , pp. 2600-2609
    • Smibert, C.A.1    Wilson, J.E.2    Kerr, K.3    Macdonald, P.M.4
  • 5
    • 0028341733 scopus 로고
    • Translational regulation of nanos by RNA localization
    • Gavis E.R., Lehmann R. Translational regulation of nanos by RNA localization. Nature 1994, 369:315-318.
    • (1994) Nature , vol.369 , pp. 315-318
    • Gavis, E.R.1    Lehmann, R.2
  • 9
    • 30744463868 scopus 로고    scopus 로고
    • The NMR and X-ray structures of the Saccharomyces cerevisiae Vts1 SAM domain define a surface for the recognition of RNA hairpins
    • Aviv T., Amborski A.N., Zhao X.S., Kwan J.J., Johnson P.E., Sicheri F., Donaldson L.W. The NMR and X-ray structures of the Saccharomyces cerevisiae Vts1 SAM domain define a surface for the recognition of RNA hairpins. J. Mol. Biol. 2006, 356:274-279.
    • (2006) J. Mol. Biol. , vol.356 , pp. 274-279
    • Aviv, T.1    Amborski, A.N.2    Zhao, X.S.3    Kwan, J.J.4    Johnson, P.E.5    Sicheri, F.6    Donaldson, L.W.7
  • 11
    • 18444383371 scopus 로고    scopus 로고
    • Protein families and RNA recognition
    • Chen Y., Varani G. Protein families and RNA recognition. FEBS J. 2005, 272:2088-2097.
    • (2005) FEBS J. , vol.272 , pp. 2088-2097
    • Chen, Y.1    Varani, G.2
  • 12
    • 0032727991 scopus 로고    scopus 로고
    • Themes in RNA-protein recognition
    • Draper D.E. Themes in RNA-protein recognition. J. Mol. Biol. 1999, 293:255-270.
    • (1999) J. Mol. Biol. , vol.293 , pp. 255-270
    • Draper, D.E.1
  • 13
    • 33846916194 scopus 로고    scopus 로고
    • L11 domain rearrangement upon binding to RNA and thiostrepton studied by NMR spectroscopy
    • Jonker H.R.A., Ilin S., Grimm S.K., Wohnert J., Schwalbe H. L11 domain rearrangement upon binding to RNA and thiostrepton studied by NMR spectroscopy. Nucleic Acids Res. 2007, 35:441-454.
    • (2007) Nucleic Acids Res. , vol.35 , pp. 441-454
    • Jonker, H.R.A.1    Ilin, S.2    Grimm, S.K.3    Wohnert, J.4    Schwalbe, H.5
  • 14
    • 0033544709 scopus 로고    scopus 로고
    • Changes in side-chain and backbone dynamics identify determinants of specificity in RNA recognition by human U1A protein
    • Mittermaier A., Varani L., Muhandiram D.R., Kay L.E., Varani G. Changes in side-chain and backbone dynamics identify determinants of specificity in RNA recognition by human U1A protein. J. Mol. Biol. 1999, 294:967-979.
    • (1999) J. Mol. Biol. , vol.294 , pp. 967-979
    • Mittermaier, A.1    Varani, L.2    Muhandiram, D.R.3    Kay, L.E.4    Varani, G.5
  • 15
    • 14844355104 scopus 로고    scopus 로고
    • Protein and RNA dynamics play key roles in determining the specific recognition of GU-rich polyadenylation regulatory elements by human Cstf-64 protein
    • Deka P., Rajan P.K., Perez-Canadillas J.M., Varani G. Protein and RNA dynamics play key roles in determining the specific recognition of GU-rich polyadenylation regulatory elements by human Cstf-64 protein. J. Mol. Biol. 2005, 347:719-733.
    • (2005) J. Mol. Biol. , vol.347 , pp. 719-733
    • Deka, P.1    Rajan, P.K.2    Perez-Canadillas, J.M.3    Varani, G.4
  • 18
    • 33646719091 scopus 로고
    • Model-free approach to the interpretation of nuclear magnetic relaxation in macromolecules. 1. Theory and range of validity
    • Lipari G., Szabo A. Model-free approach to the interpretation of nuclear magnetic relaxation in macromolecules. 1. Theory and range of validity. J. Am. Chem. Soc. 1982, 104:4546-4559.
    • (1982) J. Am. Chem. Soc. , vol.104 , pp. 4546-4559
    • Lipari, G.1    Szabo, A.2
  • 19
    • 33845553743 scopus 로고
    • Model-free approach to the interpretation of nuclear magnetic relaxation in macromolecules. 2. Analysis of experimental results
    • Lipari G., Szabo A. Model-free approach to the interpretation of nuclear magnetic relaxation in macromolecules. 2. Analysis of experimental results. J. Am. Chem. Soc. 1982, 104:4559-4570.
    • (1982) J. Am. Chem. Soc. , vol.104 , pp. 4559-4570
    • Lipari, G.1    Szabo, A.2
  • 23
    • 0024449503 scopus 로고
    • 15N inverse detected heteronuclear NMR spectroscopy-application to staphylococcal nuclease
    • 15N inverse detected heteronuclear NMR spectroscopy-application to staphylococcal nuclease. Biochemistry 1989, 28:8972-8979.
    • (1989) Biochemistry , vol.28 , pp. 8972-8979
    • Kay, L.E.1    Torchia, D.A.2    Bax, A.3
  • 25
    • 0030445011 scopus 로고    scopus 로고
    • Dynamics of ribonuclease H: temperature dependence of motions on multiple time scales
    • Mandel A.M., Akke M., Palmer A.G. Dynamics of ribonuclease H: temperature dependence of motions on multiple time scales. Biochemistry 1996, 35:16009-16023.
    • (1996) Biochemistry , vol.35 , pp. 16009-16023
    • Mandel, A.M.1    Akke, M.2    Palmer, A.G.3
  • 26
    • 0032511359 scopus 로고    scopus 로고
    • 15N chemical shift anisotropy relaxation interference: unambiguous determination of rotational diffusion tensors and chemical exchange effects in biological macromolecules
    • 15N chemical shift anisotropy relaxation interference: unambiguous determination of rotational diffusion tensors and chemical exchange effects in biological macromolecules. J. Am. Chem. Soc. 1998, 120:7905-7915.
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 7905-7915
    • Kroenke, C.D.1    Loria, J.P.2    Lee, L.K.3    Rance, M.4    Palmer, A.G.5
  • 27
    • 0032558085 scopus 로고    scopus 로고
    • 15N chemical shift anisotropy from NMR relaxation data. Ubiquitin as a test example
    • 15N chemical shift anisotropy from NMR relaxation data. Ubiquitin as a test example. J. Am. Chem. Soc. 1998, 120:7109-7110.
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 7109-7110
    • Fushman, D.1    Cowburn, D.2
  • 29
    • 17744366182 scopus 로고    scopus 로고
    • Chemical shift anisotropy tensors of carbonyl, nitrogen, and amide proton nuclei in proteins through cross-correlated relaxation in NMR spectroscopy
    • Loth K., Pelupessy P., Bodenhausen G. Chemical shift anisotropy tensors of carbonyl, nitrogen, and amide proton nuclei in proteins through cross-correlated relaxation in NMR spectroscopy. J. Am. Chem. Soc. 2005, 127:6062-6068.
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 6062-6068
    • Loth, K.1    Pelupessy, P.2    Bodenhausen, G.3
  • 30
    • 13644264053 scopus 로고    scopus 로고
    • 15N CSA magnitudes and orientations in ubiquitin are revealed by joint analysis of longitudinal and transverse NMR relaxation
    • 15N CSA magnitudes and orientations in ubiquitin are revealed by joint analysis of longitudinal and transverse NMR relaxation. J. Am. Chem. Soc. 2005, 127:1995-2005.
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 1995-2005
    • Damberg, P.1    Jarvet, J.2    Graslund, A.3
  • 33
    • 0034728579 scopus 로고    scopus 로고
    • The static magnetic field dependence of chemical exchange line-broadening defines the NMR chemical shift time scale
    • Millet O., Loria J.P., Kroenke C.D., Pons M., Palmer A.G. The static magnetic field dependence of chemical exchange line-broadening defines the NMR chemical shift time scale. J. Am. Chem. Soc. 2000, 122:2867-2877.
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 2867-2877
    • Millet, O.1    Loria, J.P.2    Kroenke, C.D.3    Pons, M.4    Palmer, A.G.5
  • 37
    • 34047136004 scopus 로고    scopus 로고
    • Global changes in local protein dynamics reduce the entropic cost of carbohydrate binding in the arabinose-binding protein
    • MacRaild C.A., Daranas A.H., Bronowska A., Homans S.W. Global changes in local protein dynamics reduce the entropic cost of carbohydrate binding in the arabinose-binding protein. J. Mol. Biol. 2007, 368:822-832.
    • (2007) J. Mol. Biol. , vol.368 , pp. 822-832
    • MacRaild, C.A.1    Daranas, A.H.2    Bronowska, A.3    Homans, S.W.4
  • 38
    • 40849102348 scopus 로고    scopus 로고
    • 15N relaxation analysis of the free and bound states of the ubiquitin-like domain of human plexin-B1 and the small GTPase Rac1
    • 15N relaxation analysis of the free and bound states of the ubiquitin-like domain of human plexin-B1 and the small GTPase Rac1. J. Mol. Biol. 2008, 377:1474-1487.
    • (2008) J. Mol. Biol. , vol.377 , pp. 1474-1487
    • Bouguet-Bonnet, S.1    Buck, M.2
  • 39
    • 0029764317 scopus 로고    scopus 로고
    • Backbone dynamics of the C-terminal domain of Escherichia coli topoisomerase I in the absence and presence of single-stranded DNA
    • Yu L.P., Zhu C.X., TseDinh Y.C., Fesik S.W. Backbone dynamics of the C-terminal domain of Escherichia coli topoisomerase I in the absence and presence of single-stranded DNA. Biochemistry 1996, 35:9661-9666.
    • (1996) Biochemistry , vol.35 , pp. 9661-9666
    • Yu, L.P.1    Zhu, C.X.2    TseDinh, Y.C.3    Fesik, S.W.4
  • 42
    • 0000660936 scopus 로고
    • Mapping of spectral density-functions using heteronuclear NMR relaxation measurements
    • Peng J.W., Wagner G. Mapping of spectral density-functions using heteronuclear NMR relaxation measurements. J. Magn. Reson. 1992, 98:308-332.
    • (1992) J. Magn. Reson. , vol.98 , pp. 308-332
    • Peng, J.W.1    Wagner, G.2
  • 45
    • 0029900275 scopus 로고    scopus 로고
    • 15N chemical shift anisotropy from quantitative measurement of relaxation interference effects
    • 15N chemical shift anisotropy from quantitative measurement of relaxation interference effects. J. Am. Chem. Soc. 1996, 118:6986-6991.
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 6986-6991
    • Tjandra, N.1    Szabo, A.2    Bax, A.3
  • 46
    • 0026748968 scopus 로고
    • 15N relaxation using inverse detected two-dimensional NMR spectroscopy: the central helix is flexible
    • 15N relaxation using inverse detected two-dimensional NMR spectroscopy: the central helix is flexible. Biochemistry 1992, 31:5269-5278.
    • (1992) Biochemistry , vol.31 , pp. 5269-5278
    • Barbato, G.1    Ikura, M.2    Kay, L.E.3    Pastor, R.W.4    Bax, A.5
  • 47
    • 0028941877 scopus 로고
    • Backbone dynamics of Escherichia coli ribonuclease HI: correlations with structure and function in an active enzyme
    • Mandel A.M., Akke M., Palmer A.G. Backbone dynamics of Escherichia coli ribonuclease HI: correlations with structure and function in an active enzyme. J. Mol. Biol. 1995, 246:144-163.
    • (1995) J. Mol. Biol. , vol.246 , pp. 144-163
    • Mandel, A.M.1    Akke, M.2    Palmer, A.G.3
  • 48
    • 0037266991 scopus 로고    scopus 로고
    • The use of model selection in the model-free analysis of protein dynamics
    • d'Auvergne E.J., Gooley P.R. The use of model selection in the model-free analysis of protein dynamics. J. Biomol. NMR 2003, 25:25-39.
    • (2003) J. Biomol. NMR , vol.25 , pp. 25-39
    • d'Auvergne, E.J.1    Gooley, P.R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.