Distance Determination in Proteins inside Xenopus laevis Oocytes by Double Electron-Electron Resonance Experiments

被引:99
作者
Igarashi, Ryuji [1 ,2 ]
Sakai, Tomomi [3 ]
Hara, Hideyuki [4 ]
Tenno, Takeshi [2 ,5 ]
Tanaka, Toshiaki [6 ]
Tochio, Hidehito [1 ,2 ]
Shirakawa, Masahiro [1 ,2 ,7 ]
机构
[1] Kyoto Univ, Grad Sch Engn, Kyoto 6158510, Japan
[2] JST, CREST, Kawaguchi, Saitama 3320012, Japan
[3] Mitsubishi Kagaku Inst Life Sci, Tokyo 1948511, Japan
[4] Bruker Biospin KK, Kanagawa 2210022, Japan
[5] Kobe Univ, Grad Sch Med, Kobe, Hyogo 6500017, Japan
[6] Tokyo Inst Technol, Fac Biosci & Biotechnol, Kanagawa 2268501, Japan
[7] Yokohama Inst, RIKEN, Kanagawa 2300045, Japan
基金
日本科学技术振兴机构;
关键词
CELL NMR-SPECTROSCOPY; ACTIVATION; ESR;
D O I
10.1021/ja906104e
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
DEER (double electron-electron resonance) enables the observation of long-range dipole interactions (1.5-8 nm) between electron spin centers and has become a unique method for structural analysis of site-directed spin-labeled (SDSL) proteins. The method was applied to proteins inside eukaryotic cells, Xenopus laevis oocytes. DEER measurements of the oocytes, into which SDSL-ubiquitin derivates were injected, gave rise to interpretable signals and allowed us to perform in situ analyses of the interspin distances of the proteins.
引用
收藏
页码:8228 / +
页数:4
相关论文
共 16 条
  • [1] High-resolution distance mapping in rhodopsin reveals the pattern of helix movement due to activation
    Altenbach, Christian
    Kusnetzow, Ana Karin
    Ernst, Oliver P.
    Hofmann, Klaus Peter
    Hubbell, Wayne L.
    [J]. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2008, 105 (21) : 7439 - 7444
  • [2] Protein structure determination using long-distance constraints from double-quantum coherence ESR: Study of T4 lysozyme
    Borbat, PP
    Mchaourab, HS
    Freed, JH
    [J]. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 2002, 124 (19) : 5304 - 5314
  • [3] Mapping structural interactions using in-cell NMR spectroscopy (STINT-NMR)
    Burz, DS
    Dutta, K
    Cowburn, D
    Shekhtman, A
    [J]. NATURE METHODS, 2006, 3 (02) : 91 - 93
  • [4] The determination of pair distance distributions by pulsed ESR using Tikhonov regularization
    Chiang, YW
    Borbat, PP
    Freed, JH
    [J]. JOURNAL OF MAGNETIC RESONANCE, 2005, 172 (02) : 279 - 295
  • [5] Ferrell JE, 1999, BIOESSAYS, V21, P833, DOI 10.1002/(SICI)1521-1878(199910)21:10<833::AID-BIES5>3.0.CO
  • [6] 2-P
  • [7] DETERMINATION OF LOCAL PROTEIN-STRUCTURE BY SPIN-LABEL DIFFERENCE 2D NMR - THE REGION NEIGHBORING ASP61 OF SUBUNIT-C OF THE F1F0 ATP SYNTHASE
    GIRVIN, ME
    FILLINGAME, RH
    [J]. BIOCHEMISTRY, 1995, 34 (05) : 1635 - 1645
  • [8] High-resolution multi-dimensional NMR spectroscopy of proteins in human cells
    Inomata, Kohsuke
    Ohno, Ayako
    Tochio, Hidehito
    Isogai, Shin
    Tenno, Takeshi
    Nakase, Ikuhiko
    Takeuchi, Toshihide
    Futaki, Shiroh
    Ito, Yutaka
    Hiroaki, Hidekazu
    Shirakawa, Masahiro
    [J]. NATURE, 2009, 458 (7234) : 106 - U11
  • [9] DeerAnalysis2006 - a comprehensive software package for analyzing pulsed ELDOR data
    Jeschke, G.
    Chechik, V.
    Ionita, P.
    Godt, A.
    Zimmermann, H.
    Banham, J.
    Timmel, C. R.
    Hilger, D.
    Jung, H.
    [J]. APPLIED MAGNETIC RESONANCE, 2006, 30 (3-4) : 473 - 498
  • [10] Differential dynamical effects of macromolecular crowding on an intrinsically disordered protein and a globular protein: Implications for in-cell NMR spectroscopy
    Li, Conggang
    Charlton, Lisa M.
    Lakkavaram, Asha
    Seagle, Christopher
    Wang, Guifang
    Young, Gregory B.
    Macdonald, Jeffrey M.
    Pielak, Gary J.
    [J]. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 2008, 130 (20) : 6310 - +