메뉴 건너뛰기




Volumn 22, Issue 4, 2014, Pages 526-538

Nucleotides and substrates trigger the dynamics of the Toc34 GTPase homodimer involved in chloroplast preprotein translocation

Author keywords

[No Author keywords available]

Indexed keywords

ARGININE; ENZYME VARIANT; GUANOSINE TRIPHOSPHATASE; GUANOSINE TRIPHOSPHATE; HOMODIMER; NUCLEOTIDE; PROTEIN PRECURSOR; PROTEIN TOC34; UNCLASSIFIED DRUG; CHLOROPLAST PROTEIN; NUCLEOTIDE DERIVATIVE; TOC34 PROTEIN; GUANOSINE DIPHOSPHATE; MEMBRANE PROTEIN; PROTEIN BINDING; RECOMBINANT PROTEIN; TOC34 PROTEIN, PLANT; VEGETABLE PROTEIN;

EID: 84898452079     PISSN: 09692126     EISSN: 18784186     Source Type: Journal    
DOI: 10.1016/j.str.2014.02.004     Document Type: Article
Times cited : (21)

References (57)
  • 1
    • 33646377416 scopus 로고    scopus 로고
    • Separating structural heterogeneities from stochastic variations in fluorescence resonance energy transfer distributions via photon distribution analysis
    • M. Antonik, S. Felekyan, A. Gaiduk, and C.A. Seidel Separating structural heterogeneities from stochastic variations in fluorescence resonance energy transfer distributions via photon distribution analysis J. Phys. Chem. B 110 2006 6970 6978
    • (2006) J. Phys. Chem. B , vol.110 , pp. 6970-6978
    • Antonik, M.1    Felekyan, S.2    Gaiduk, A.3    Seidel, C.A.4
  • 2
    • 77954434270 scopus 로고    scopus 로고
    • Nucleotide binding and dimerization at the chloroplast pre-protein import receptor, atToc33, are not essential in vivo but do increase import efficiency
    • H. Aronsson, J. Combe, R. Patel, B. Agne, M. Martin, F. Kessler, and P. Jarvis Nucleotide binding and dimerization at the chloroplast pre-protein import receptor, atToc33, are not essential in vivo but do increase import efficiency Plant J. 63 2010 297 311
    • (2010) Plant J. , vol.63 , pp. 297-311
    • Aronsson, H.1    Combe, J.2    Patel, R.3    Agne, B.4    Martin, M.5    Kessler, F.6    Jarvis, P.7
  • 6
    • 57749201550 scopus 로고    scopus 로고
    • PH sensitivity of the GTPase Toc33 as a regulatory circuit for protein translocation into chloroplasts
    • T. Bionda, P. Koenig, M. Oreb, I. Tews, and E. Schleiff pH sensitivity of the GTPase Toc33 as a regulatory circuit for protein translocation into chloroplasts Plant Cell Physiol. 49 2008 1917 1921
    • (2008) Plant Cell Physiol. , vol.49 , pp. 1917-1921
    • Bionda, T.1    Koenig, P.2    Oreb, M.3    Tews, I.4    Schleiff, E.5
  • 7
    • 77952787295 scopus 로고    scopus 로고
    • Stabilization of G domain conformations in the tRNA-modifying MnmE-GidA complex observed with double electron electron resonance spectroscopy
    • S. Böhme, S. Meyer, A. Krüger, H.J. Steinhoff, A. Wittinghofer, and J.P. Klare Stabilization of G domain conformations in the tRNA-modifying MnmE-GidA complex observed with double electron electron resonance spectroscopy J. Biol. Chem. 285 2010 16991 17000
    • (2010) J. Biol. Chem. , vol.285 , pp. 16991-17000
    • Böhme, S.1    Meyer, S.2    Krüger, A.3    Steinhoff, H.J.4    Wittinghofer, A.5    Klare, J.P.6
  • 9
    • 34249018367 scopus 로고    scopus 로고
    • GEFs and GAPs: Critical elements in the control of small G proteins
    • J.L. Bos, H. Rehmann, and A. Wittinghofer GEFs and GAPs: critical elements in the control of small G proteins Cell 129 2007 865 877
    • (2007) Cell , vol.129 , pp. 865-877
    • Bos, J.L.1    Rehmann, H.2    Wittinghofer, A.3
  • 10
    • 77953023419 scopus 로고    scopus 로고
    • G domain dimerization controls dynamin's assembly-stimulated GTPase activity
    • J.S. Chappie, S. Acharya, M. Leonard, S.L. Schmid, and F. Dyda G domain dimerization controls dynamin's assembly-stimulated GTPase activity Nature 465 2010 435 440
    • (2010) Nature , vol.465 , pp. 435-440
    • Chappie, J.S.1    Acharya, S.2    Leonard, M.3    Schmid, S.L.4    Dyda, F.5
  • 11
    • 21744432683 scopus 로고    scopus 로고
    • GDIs: Central regulatory molecules in Rho GTPase activation
    • C. DerMardirossian, and G.M. Bokoch GDIs: central regulatory molecules in Rho GTPase activation Trends Cell Biol. 15 2005 356 363
    • (2005) Trends Cell Biol. , vol.15 , pp. 356-363
    • Dermardirossian, C.1    Bokoch, G.M.2
  • 13
    • 80053376521 scopus 로고    scopus 로고
    • The crystal structure of dynamin
    • M.G.J. Ford, S. Jenni, and J. Nunnari The crystal structure of dynamin Nature 477 2011 561 566
    • (2011) Nature , vol.477 , pp. 561-566
    • Ford, M.G.J.1    Jenni, S.2    Nunnari, J.3
  • 14
    • 70350602056 scopus 로고    scopus 로고
    • The structure of the ribosome with elongation factor G trapped in the posttranslocational state
    • Y.G. Gao, M. Selmer, C.M. Dunham, A. Weixlbaumer, A.C. Kelley, and V. Ramakrishnan The structure of the ribosome with elongation factor G trapped in the posttranslocational state Science 326 2009 694 699
    • (2009) Science , vol.326 , pp. 694-699
    • Gao, Y.G.1    Selmer, M.2    Dunham, C.M.3    Weixlbaumer, A.4    Kelley, A.C.5    Ramakrishnan, V.6
  • 16
    • 79952065943 scopus 로고    scopus 로고
    • GTPase activity of Di-Ras proteins is stimulated by Rap1GAP proteins
    • R. Gasper, B. Sot, and A. Wittinghofer GTPase activity of Di-Ras proteins is stimulated by Rap1GAP proteins Small GTPases 1 2010 133 141
    • (2010) Small GTPases , vol.1 , pp. 133-141
    • Gasper, R.1    Sot, B.2    Wittinghofer, A.3
  • 18
    • 0028349917 scopus 로고
    • Characterization of the active site of p21 ras by electron spin-echo envelope modulation spectroscopy with selective labeling: Comparisons between GDP and GTP forms
    • C.J. Halkides, C.T. Farrar, R.G. Larsen, A.G. Redfield, and D.J. Singel Characterization of the active site of p21 ras by electron spin-echo envelope modulation spectroscopy with selective labeling: comparisons between GDP and GTP forms Biochemistry 33 1994 4019 4035
    • (1994) Biochemistry , vol.33 , pp. 4019-4035
    • Halkides, C.J.1    Farrar, C.T.2    Larsen, R.G.3    Redfield, A.G.4    Singel, D.J.5
  • 19
    • 23644451172 scopus 로고    scopus 로고
    • Crystal structure of a mutant elongation factor G trapped with a GTP analogue
    • S. Hansson, R. Singh, A.T. Gudkov, A. Liljas, and D.T. Logan Crystal structure of a mutant elongation factor G trapped with a GTP analogue FEBS Lett. 579 2005 4492 4497
    • (2005) FEBS Lett. , vol.579 , pp. 4492-4497
    • Hansson, S.1    Singh, R.2    Gudkov, A.T.3    Liljas, A.4    Logan, D.T.5
  • 20
    • 70450176713 scopus 로고    scopus 로고
    • Transport vesicle formation in plant cells
    • I. Hwang, and D.G. Robinson Transport vesicle formation in plant cells Curr. Opin. Plant Biol. 12 2009 660 669
    • (2009) Curr. Opin. Plant Biol. , vol.12 , pp. 660-669
    • Hwang, I.1    Robinson, D.G.2
  • 21
    • 33645742291 scopus 로고    scopus 로고
    • Nucleotide exchange via local protein unfolding - Structure of Rab8 in complex with MSS4
    • A. Itzen, O. Pylypenko, R.S. Goody, K. Alexandrov, and A. Rak Nucleotide exchange via local protein unfolding - structure of Rab8 in complex with MSS4 EMBO J. 25 2006 1445 1455
    • (2006) EMBO J. , vol.25 , pp. 1445-1455
    • Itzen, A.1    Pylypenko, O.2    Goody, R.S.3    Alexandrov, K.4    Rak, A.5
  • 22
    • 12244310188 scopus 로고    scopus 로고
    • The chloroplast import receptor Toc34 functions as preprotein-regulated GTPase
    • M. Jelic, N. Sveshnikova, M. Motzkus, P. Hörth, J. Soll, and E. Schleiff The chloroplast import receptor Toc34 functions as preprotein-regulated GTPase Biol. Chem. 383 2002 1875 1883
    • (2002) Biol. Chem. , vol.383 , pp. 1875-1883
    • Jelic, M.1    Sveshnikova, N.2    Motzkus, M.3    Hörth, P.4    Soll, J.5    Schleiff, E.6
  • 24
    • 33645717179 scopus 로고    scopus 로고
    • Characterization of the preprotein translocon at the outer envelope membrane of chloroplasts by blue native PAGE
    • S. Kikuchi, T. Hirohashi, and M. Nakai Characterization of the preprotein translocon at the outer envelope membrane of chloroplasts by blue native PAGE Plant Cell Physiol. 47 2006 363 371
    • (2006) Plant Cell Physiol. , vol.47 , pp. 363-371
    • Kikuchi, S.1    Hirohashi, T.2    Nakai, M.3
  • 25
    • 41449086856 scopus 로고    scopus 로고
    • The GTPase cycle of the chloroplast import receptors Toc33/Toc34: Implications from monomeric and dimeric structures
    • P. Koenig, M. Oreb, A. Höfle, S. Kaltofen, K. Rippe, I. Sinning, E. Schleiff, and I. Tews The GTPase cycle of the chloroplast import receptors Toc33/Toc34: implications from monomeric and dimeric structures Structure 16 2008 585 596
    • (2008) Structure , vol.16 , pp. 585-596
    • Koenig, P.1    Oreb, M.2    Höfle, A.3    Kaltofen, S.4    Rippe, K.5    Sinning, I.6    Schleiff, E.7    Tews, I.8
  • 27
    • 71449100363 scopus 로고    scopus 로고
    • Toc receptor dimerization participates in the initiation of membrane translocation during protein import into chloroplasts
    • J.H. Lee, F. Wang, and D.J. Schnell Toc receptor dimerization participates in the initiation of membrane translocation during protein import into chloroplasts J. Biol. Chem. 284 2009 31130 31141
    • (2009) J. Biol. Chem. , vol.284 , pp. 31130-31141
    • Lee, J.H.1    Wang, F.2    Schnell, D.J.3
  • 28
    • 0036295212 scopus 로고    scopus 로고
    • Classification and evolution of P-loop GTPases and related ATPases
    • D.D. Leipe, Y.I. Wolf, E.V. Koonin, and L. Aravind Classification and evolution of P-loop GTPases and related ATPases J. Mol. Biol. 317 2002 41 72
    • (2002) J. Mol. Biol. , vol.317 , pp. 41-72
    • Leipe, D.D.1    Wolf, Y.I.2    Koonin, E.V.3    Aravind, L.4
  • 29
    • 84868228819 scopus 로고    scopus 로고
    • Chloroplast biogenesis is regulated by direct action of the ubiquitin-proteasome system
    • Q.H. Ling, W.H. Huang, A. Baldwin, and P. Jarvis Chloroplast biogenesis is regulated by direct action of the ubiquitin-proteasome system Science 338 2012 655 659
    • (2012) Science , vol.338 , pp. 655-659
    • Ling, Q.H.1    Huang, W.H.2    Baldwin, A.3    Jarvis, P.4
  • 30
    • 70350520515 scopus 로고    scopus 로고
    • Kissing G domains of MnmE monitored by X-ray crystallography and pulse electron paramagnetic resonance spectroscopy
    • S. Meyer, S. Böhme, A. Krüger, H.J. Steinhoff, J.P. Klare, and A. Wittinghofer Kissing G domains of MnmE monitored by X-ray crystallography and pulse electron paramagnetic resonance spectroscopy PLoS Biol. 7 2009 e1000212
    • (2009) PLoS Biol. , vol.7 , pp. 1000212
    • Meyer, S.1    Böhme, S.2    Krüger, A.3    Steinhoff, H.J.4    Klare, J.P.5    Wittinghofer, A.6
  • 31
    • 0002279727 scopus 로고
    • Electron-electron double resonance in electron spin echo: Model biradical systems and the sensitized photolysis of decalin
    • A.D. Milov, A.B. Ponomarev, and Y.D. Tsvetkov Electron-electron double resonance in electron spin echo: model biradical systems and the sensitized photolysis of decalin Chem. Phys. Lett. 110 1984 67 72
    • (1984) Chem. Phys. Lett. , vol.110 , pp. 67-72
    • Milov, A.D.1    Ponomarev, A.B.2    Tsvetkov, Y.D.3
  • 35
    • 79952104930 scopus 로고    scopus 로고
    • Septin structure and function in yeast and beyond
    • Y. Oh, and E. Bi Septin structure and function in yeast and beyond Trends Cell Biol. 21 2011 141 148
    • (2011) Trends Cell Biol. , vol.21 , pp. 141-148
    • Oh, Y.1    Bi, E.2
  • 37
    • 0034132251 scopus 로고    scopus 로고
    • Dead-time free measurement of dipole-dipole interactions between electron spins
    • M. Pannier, S. Veit, A. Godt, G. Jeschke, and H.W. Spiess Dead-time free measurement of dipole-dipole interactions between electron spins J. Magn. Reson. 142 2000 331 340
    • (2000) J. Magn. Reson. , vol.142 , pp. 331-340
    • Pannier, M.1    Veit, S.2    Godt, A.3    Jeschke, G.4    Spiess, H.W.5
  • 38
    • 79251562868 scopus 로고    scopus 로고
    • Rotamer libraries of spin labelled cysteines for protein studies
    • Y. Polyhach, E. Bordignon, and G. Jeschke Rotamer libraries of spin labelled cysteines for protein studies Phys. Chem. Chem. Phys. 13 2011 2356 2366
    • (2011) Phys. Chem. Chem. Phys. , vol.13 , pp. 2356-2366
    • Polyhach, Y.1    Bordignon, E.2    Jeschke, G.3
  • 39
    • 84856022421 scopus 로고    scopus 로고
    • Heat shock protein 90's mechanochemical cycle is dominated by thermal fluctuations
    • C. Ratzke, F. Berkemeier, and T. Hugel Heat shock protein 90's mechanochemical cycle is dominated by thermal fluctuations Proc. Natl. Acad. Sci. USA 109 2012 161 166
    • (2012) Proc. Natl. Acad. Sci. USA , vol.109 , pp. 161-166
    • Ratzke, C.1    Berkemeier, F.2    Hugel, T.3
  • 41
    • 44449134820 scopus 로고    scopus 로고
    • A practical guide to single-molecule FRET
    • R. Roy, S. Hohng, and T. Ha A practical guide to single-molecule FRET Nat. Methods 5 2008 507 516
    • (2008) Nat. Methods , vol.5 , pp. 507-516
    • Roy, R.1    Hohng, S.2    Ha, T.3
  • 42
    • 0032127912 scopus 로고    scopus 로고
    • GTPase-activating proteins: Helping hands to complement an active site
    • K. Scheffzek, M.R. Ahmadian, and A. Wittinghofer GTPase-activating proteins: helping hands to complement an active site Trends Biochem. Sci. 23 1998 257 262
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 257-262
    • Scheffzek, K.1    Ahmadian, M.R.2    Wittinghofer, A.3
  • 43
    • 34548317408 scopus 로고    scopus 로고
    • Long-range distance determinations in biomacromolecules by EPR spectroscopy
    • O. Schiemann, and T.F. Prisner Long-range distance determinations in biomacromolecules by EPR spectroscopy Q. Rev. Biophys. 40 2007 1 53
    • (2007) Q. Rev. Biophys. , vol.40 , pp. 1-53
    • Schiemann, O.1    Prisner, T.F.2
  • 44
    • 78650517733 scopus 로고    scopus 로고
    • Common ground for protein translocation: Access control for mitochondria and chloroplasts
    • E. Schleiff, and T. Becker Common ground for protein translocation: access control for mitochondria and chloroplasts Nat. Rev. Mol. Cell Biol. 12 2011 48 59
    • (2011) Nat. Rev. Mol. Cell Biol. , vol.12 , pp. 48-59
    • Schleiff, E.1    Becker, T.2
  • 45
    • 0037065694 scopus 로고    scopus 로고
    • Structural and guanosine triphosphate/diphosphate requirements for transit peptide recognition by the cytosolic domain of the chloroplast outer envelope receptor, Toc34
    • E. Schleiff, J. Soll, N. Sveshnikova, R. Tien, S. Wright, C. Dabney-Smith, C. Subramanian, and B.D. Bruce Structural and guanosine triphosphate/diphosphate requirements for transit peptide recognition by the cytosolic domain of the chloroplast outer envelope receptor, Toc34 Biochemistry 41 2002 1934 1946
    • (2002) Biochemistry , vol.41 , pp. 1934-1946
    • Schleiff, E.1    Soll, J.2    Sveshnikova, N.3    Tien, R.4    Wright, S.5    Dabney-Smith, C.6    Subramanian, C.7    Bruce, B.D.8
  • 46
    • 0037450662 scopus 로고    scopus 로고
    • Characterization of the translocon of the outer envelope of chloroplasts
    • E. Schleiff, J. Soll, M. Küchler, W. Kühlbrandt, and R. Harrer Characterization of the translocon of the outer envelope of chloroplasts J. Cell Biol. 160 2003 541 551
    • (2003) J. Cell Biol. , vol.160 , pp. 541-551
    • Schleiff, E.1    Soll, J.2    Küchler, M.3    Kühlbrandt, W.4    Harrer, R.5
  • 47
    • 70349451648 scopus 로고    scopus 로고
    • Molecular interactions within the plant TOC complex
    • M.S. Sommer, and E. Schleiff Molecular interactions within the plant TOC complex Biol. Chem. 390 2009 739 744
    • (2009) Biol. Chem. , vol.390 , pp. 739-744
    • Sommer, M.S.1    Schleiff, E.2
  • 51
    • 0034603196 scopus 로고    scopus 로고
    • Large-scale movement of elongation factor G and extensive conformational change of the ribosome during translocation
    • H. Stark, M.V. Rodnina, H.J. Wieden, M. van Heel, and W. Wintermeyer Large-scale movement of elongation factor G and extensive conformational change of the ribosome during translocation Cell 100 2000 301 309
    • (2000) Cell , vol.100 , pp. 301-309
    • Stark, H.1    Rodnina, M.V.2    Wieden, H.J.3    Van Heel, M.4    Wintermeyer, W.5
  • 53
    • 33748785471 scopus 로고    scopus 로고
    • Role and timing of GTP binding and hydrolysis during EF-G-dependent tRNA translocation on the ribosome
    • B. Wilden, A. Savelsbergh, M.V. Rodnina, and W. Wintermeyer Role and timing of GTP binding and hydrolysis during EF-G-dependent tRNA translocation on the ribosome Proc. Natl. Acad. Sci. USA 103 2006 13670 13675
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 13670-13675
    • Wilden, B.1    Savelsbergh, A.2    Rodnina, M.V.3    Wintermeyer, W.4
  • 54
    • 79959393264 scopus 로고    scopus 로고
    • Structure-function relationships of the G domain, a canonical switch motif
    • A. Wittinghofer, and I.R. Vetter Structure-function relationships of the G domain, a canonical switch motif Annu. Rev. Biochem. 80 2011 943 971
    • (2011) Annu. Rev. Biochem. , vol.80 , pp. 943-971
    • Wittinghofer, A.1    Vetter, I.R.2
  • 55
    • 55849131745 scopus 로고    scopus 로고
    • Cell polarity signaling in Arabidopsis
    • Z. Yang Cell polarity signaling in Arabidopsis Annu. Rev. Cell Dev. Biol. 24 2008 551 575
    • (2008) Annu. Rev. Cell Dev. Biol. , vol.24 , pp. 551-575
    • Yang, Z.1
  • 57
    • 64849092676 scopus 로고    scopus 로고
    • Legume small GTPases and their role in the establishment of symbiotic associations with Rhizobium spp
    • B. Yuksel, and A.R. Memon Legume small GTPases and their role in the establishment of symbiotic associations with Rhizobium spp Plant Signal. Behav. 4 2009 257 260
    • (2009) Plant Signal. Behav. , vol.4 , pp. 257-260
    • Yuksel, B.1    Memon, A.R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.