메뉴 건너뛰기




Volumn 461, Issue 7260, 2009, Pages 60-65

Structures of the tRNA export factor in the nuclear and cytosolic states

Author keywords

[No Author keywords available]

Indexed keywords

EXPORTIN 1; GUANOSINE TRIPHOSPHATE; TRANSFER RNA;

EID: 69949094998     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature08394     Document Type: Article
Times cited : (104)

References (53)
  • 1
    • 34648816826 scopus 로고    scopus 로고
    • Exporting RNA from the nucleus to the cytoplasm
    • Kohler, A. & Hurt, E. Exporting RNA from the nucleus to the cytoplasm, Nature Rev. Mol. Cell Biol. 8, 761-773 (2007).
    • (2007) Nature Rev. Mol. Cell Biol. , vol.8
    • Kohler, A.1    Hurt, E.2
  • 4
    • 39149125768 scopus 로고    scopus 로고
    • Towards reconciling structure and function in the nuclear pore complex
    • Lim, R. Y., Aebi, U. & Fahrenkrog, B. Towards reconciling structure and function in the nuclear pore complex, Histochem. Cell Biol. 129,.105-116 (2008).
    • (2008) Histochem. Cell Biol. , vol.129
    • Lim, R.Y.1    Aebi, U.2    Fahrenkrog, B.3
  • 5
    • 65449152302 scopus 로고    scopus 로고
    • Translocation through the nuclear pore: Kaps pave the way
    • Peters, R., Translocation through the nuclear pore: Kaps pave the way, Bioessays 31, 466-477 (2009).
    • (2009) Bioessays , vol.31
    • Peters, R.1
  • 7
    • 0032510462 scopus 로고    scopus 로고
    • Identification of a nuclear export receptor for tRNA
    • 7. Arts, G. J., Fornerod, M. & Mattaj, I. W. Identification of a nuclear export receptor for tRNA, Curr. Biol. 8, 305-314 (1998). (Pubitemid 28159116)
    • (1998) Current Biology , vol.8 , Issue.6
    • Arts, G.-J.1    Fornerod, M.2    Mattaj, I.W.3
  • 10
    • 34548627531 scopus 로고    scopus 로고
    • Structural biology of nucleocytoplasmic transport
    • Cook, A., Bono, F., Jinek, M. & Conti, E. Structural biology of nucleocytoplasmic transport, Annu. Rev. Biochem. 76, 647-671 (2007),
    • (2007) Annu. Rev. Biochem. , vol.76
    • Cook, A.1    Bono, F.2    Jinek, M.3    Conti, E.4
  • 11
    • 33645015535 scopus 로고    scopus 로고
    • Nuclear transport is becoming crystal clear
    • Madrid, A. S. & Weis, K. Nuclear transport is becoming crystal clear.Chromosoma 115, 98-109(2006).
    • (2006) Chromosoma , vol.115
    • Madrid, A.S.1    Weis, K.2
  • 12
    • 0037112842 scopus 로고    scopus 로고
    • Exportin-5-mediated nuclear export of eukaryotic elongation factor 1A and tRNA
    • DOI 10.1093/emboj/cdf620
    • 12. Calado, A., Treichel, N., Muller, E. C., Otto, A, & Kutay, U. Exportin-5-mediated nuclear export of eukaryotic elongation factor 1A and tRNA, EMBO J. 21, 6216-6224(2002), (Pubitemid 35415338)
    • (2002) EMBO Journal , vol.21 , Issue.22
    • Calado, A.1    Treichel, N.2    Muller, E.-C.3    Otto, A.4    Kutay, U.5
  • 15
    • 0033862354 scopus 로고    scopus 로고
    • The crystal structure of yeast phenylalanine tRNA at 1.93 A resolution: A classic structure revisited
    • DOI 10.1017/S1355838200000364
    • 15. Shi, H. & Moore, P. B. The crystal structure of yeast phenylalanine tRNA at 1.93 Ä resolution: a classic structure revisited, RNA 6, 1091-1105 (2000). (Pubitemid 30620393)
    • (2000) RNA , vol.6 , Issue.8
    • Shi, H.1    Moore, P.B.2
  • 16
    • 62549165191 scopus 로고    scopus 로고
    • RNase P: Increased versatility through protein complexity?
    • Marvin, M. C. & Engelke, D. R. RNase P: increased versatility through protein complexity? RNA Biol. 6, 40-42 (2009).
    • (2009) RNA Biol. , vol.6
    • Marvin, M.C.1    Engelke, D.R.2
  • 18
    • 32344447144 scopus 로고    scopus 로고
    • A story with a good ending: TRNA 3′-end maturation by CCA-adding enzymes
    • DOI 10.1016/j.sbi.2005.12.001, PII S0959440X05002204
    • 18. Xiong, Y. & Steltz, T. A. A story with a good ending: tRNA 3'-end maturation by CCA-addlng enzymes, Curr. Opin. Struct. Biol. 16, 12-17 (2006). (Pubitemid 43221866)
    • (2006) Current Opinion in Structural Biology , vol.16 , Issue.1
    • Xiong, Y.1    Steitz, T.A.2
  • 19
    • 0032509304 scopus 로고    scopus 로고
    • Proofreading and aminoacylation of tRNAs before export from the nucleus
    • DOI 10.1126/science.282.5396.2082
    • 19. Lund, E. & Dahlberg, J. E. Proofreading and aminoacylation of tRNAs before export from the nucleus, Science 282, 2082-2085 (1998). (Pubitemid 29001264)
    • (1998) Science , vol.282 , Issue.5396
    • Lund, E.1    Dahlberg, J.E.2
  • 20
    • 0023083423 scopus 로고
    • Transfer RNA modification
    • Bjork, G. R. et al. Transfer RNA modification, Annu. Rev, Biochem. 56, 263-287 (1987)
    • (1987) Annu. Rev, Biochem. , vol.56
    • Bjork, G.R.1
  • 21
    • 43049099252 scopus 로고    scopus 로고
    • An embarrassment of riches: The enzymology of RNA modification
    • Iwata-Reuyl, D. An embarrassment of riches: the enzymology of RNA modification, Curr. Opin. Chem. Biol. 12, 126-133 (2008).
    • (2008) Curr. Opin. Chem. Biol. , vol.12
    • Iwata-Reuyl, D.1
  • 22
    • 0032535450 scopus 로고    scopus 로고
    • The role of exportin-t in selective nuclear export of mature tRNAs
    • Arts, G. J., Kuersten, S., Romby, P., Ehresmann, B.& Mattaj, I. W. The role of exportin-t in selective nuclear export of mature tRNAs, EMSO J. 17, 7430-7441 (1998).
    • (1998) EMSO J. , vol.17
    • Arts, G.J.1    Kuersten, S.2    Romby, P.3    Ehresmann, B.4    Mattaj, I.W.5
  • 24
    • 0001506297 scopus 로고    scopus 로고
    • Structure of the nuclear transport complex karyopherin-β2- Ran·GppNHp
    • DOI 10.1038/20375
    • 24. Chook, Y. M. & Blobel, G. Structure of the nuclear transport complex karyopherinβ2-Ran' GppNHp. Nature 399, 230-237 (1999). (Pubitemid 29246446)
    • (1999) Nature , vol.399 , Issue.6733
    • Chook, Y.M.1    Blobel, G.2
  • 25
    • 20444468112 scopus 로고    scopus 로고
    • Structural basis for nuclear import complex dissociation by RanGTP
    • DOI 10.1038/nature03578
    • 25. Lee, S. J., Matsuura, Y., Liu, S. M. & Stewart, M. Structural basis for nuclear import complex dissociation by RanGTP. Nature 435, 693-696 (2005). (Pubitemid 40825515)
    • (2005) Nature , vol.435 , Issue.7042
    • Lee, S.J.1    Matsuura, Y.2    Liu, S.M.3    Stewart, M.4
  • 26
    • 11144257756 scopus 로고    scopus 로고
    • Structural basis for the assembly of a nuclear export complex
    • DOI 10.1038/nature03144
    • 26. Matsuura, Y. & Stewart, M. Structural basis for the assembly of a nuclear export complex, Nature 432, 872-877 (2004). (Pubitemid 40037144)
    • (2004) Nature , vol.432 , Issue.7019
    • Matsuura, Y.1    Stewart, M.2
  • 27
    • 66249108600 scopus 로고    scopus 로고
    • Crystal structure of the nuclear export receptor CRMI in complex with Snurportinl and RanGTP
    • Monecke, T. et al. Crystal structure of the nuclear export receptor CRMI in complex with Snurportinl and RanGTP, Science 324, 1087-1091 (2009).
    • (2009) Science , vol.324
    • Monecke, T.1
  • 30
    • 0033612390 scopus 로고    scopus 로고
    • Structural view of the Ran-importin β interaction at 2.3 A resolution
    • DOI 10.1016/S0092-8674(00)80774-6
    • 30. Vetter, I. R., Arndt, A., Kutay, U., Gorllch, D., & Wittinghofer, A. Structural view of the Ran-lmportln β interaction at 2.3AÅ resolution, Cell 97, 635-646 (1999). (Pubitemid 29256966)
    • (1999) Cell , vol.97 , Issue.5
    • Vetter, I.R.1    Arndt, A.2    Kutay, U.3    Gorlich, D.4    Wittinghofer, A.5
  • 32
    • 0033587167 scopus 로고    scopus 로고
    • Structure of importin-β bound to the IBB domain of importin-β
    • DOI 10.1038/20367
    • 32. CIngolanI, G., Petosa, C., Weis, K. & Müller, C. W. Structure of importin-β bound to the IBB domain of importin-α, Nature 399, 221-229 (1999). (Pubitemid 29246445)
    • (1999) Nature , vol.399 , Issue.6733
    • Cingolani, G.1    Petosa, C.2    Weis, K.3    Muller, C.W.4
  • 33
    • 0036316102 scopus 로고    scopus 로고
    • Steady-state nuclear localization of exportin-t involves RanGTP binding and two distinct nuclear pore complex interaction domains
    • DOI 10.1128/MCB.22.16.5708-5720.2002
    • 33. Kuersten, S., Arts, G. J., Walther, T. C. Englmeier, L. & Mattaj, I. W. Steady-state nuclear localization of exportin-t involves RanGTP binding and two distinct nuclear pore complex interaction domains, MoI. Cell. Biol. 22, 5708-5720 (2002). (Pubitemid 34815821)
    • (2002) Molecular and Cellular Biology , vol.22 , Issue.16
    • Kuersten, S.1    Arts, G.-J.2    Walther, T.C.3    Englmeier, L.4    Mattaj, I.W.5
  • 36
    • 20844458749 scopus 로고    scopus 로고
    • The structure of the nuclear export receptor Cse1 in its cytosolic state reveals a closed conformation incompatible with cargo binding
    • DOI 10.1016/j.molcel.2005.03.021, PII S1097276505012153
    • 36. Cook, A. et al. The structure of the nuclear export receptor Csel in its cytosolic state reveals a closed conformation incompatible with cargo binding, MoI. Cell 18, 355-367 (2005). (Pubitemid 41350540)
    • (2005) Molecular Cell , vol.18 , Issue.3
    • Cook, A.1    Fernandez, E.2    Lindner, D.3    Ebert, J.4    Schlenstedt, G.5    Conti, E.6
  • 37
    • 66149092358 scopus 로고    scopus 로고
    • Structural basis for assembly and disassembly of the CRMI nuclear export complex
    • Dong, X., Biswas, A. & Chook, Y. M. Structural basis for assembly and disassembly of the CRMI nuclear export complex, Nature Struct. Mol. Biol. 16, 558-560 (2009).
    • (2009) Nature Struct. Mol. Biol. , vol.16
    • Dong, X.1    Biswas, A.2    Chook, Y.M.3
  • 38
    • 0026591001 scopus 로고
    • Structural and functional relationships between aminoacyl-tRNA synthetases
    • Moras, D. Structural and functional relationships between aminoacyl-tRNA synthetases, Trends Biochem. Sci. 17, 159-164 (1992).
    • (1992) Trends Biochem. Sci. , vol.17
    • Moras, D.1
  • 39
    • 0022273106 scopus 로고
    • 1H-15N heteronuclear NMR studies of Escherichia coli thloredoxln in samples isotoplcally labeled by residue type
    • LeMaster, D. M. & Richards, F. M. 1H-15N heteronuclear NMR studies of Escherichia coli thloredoxln In samples isotoplcally labeled by residue type, Biochemistry 24, 7263-7268 (1985).
    • (1985) Biochemistry , vol.24
    • Lemaster, D.M.1    Richards, F.M.2
  • 40
    • 0028228301 scopus 로고
    • Efficient and rapid affinity purification of proteins using recombinant fusion proteases
    • Walker, P. A. et al. Efficient and rapid affinity purification of proteins using recombinant fusion proteases, Biotechnology 12, 601-605 (1994).
    • (1994) Biotechnology , vol.12
    • Walker, P.A.1
  • 41
    • 0029916726 scopus 로고    scopus 로고
    • Crystallization and preliminary X-rayanalysIsofthe9 kDa protein of the mouse signal recognition particle and the selenomethionyl-SRP9
    • Doublle, S. et al. Crystallization and preliminary X-rayanalysIsofthe9 kDa protein of the mouse signal recognition particle and the selenomethionyl-SRP9. FESS Left 384, 219-221 (1996).
    • (1996) FESS Left , vol.384
    • Doublle, S.1
  • 43
    • 0028103275 scopus 로고
    • Collaborative Computational Project, Number 4, the CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project, Number 4, The CCP4 suite: programs for protein crystallography, Acta Crystallogr. D 50, 760-763 (1994).
    • (1994) Acta Crystallogr. D , vol.50
  • 45
    • 0027879008 scopus 로고
    • Automatic processing of rotation diffraction data from crystalsof Initially unknown symmetry and cell constants
    • Kabsch, W. Automatic processing of rotation diffraction data from crystalsof Initially unknown symmetry and cell constants, J. Appl. Crystallogr. 26, 795-800 (1993).
    • (1993) J. Appl. Crystallogr. , vol.26
    • Kabsch, W.1
  • 48
    • 34447508216 scopus 로고    scopus 로고
    • Phaser crystallographic software
    • McCoy, A. J. et al. Phaser crystallographic software, J. Appl. Crystallogr. 40, 658-674 (2007).
    • (2007) J. Appl. Crystallogr. , vol.40
    • McCoy, A.J.1
  • 49
    • 43749083257 scopus 로고    scopus 로고
    • Chainsaw: A program for mutating pdb files used as templates in molecular replacement
    • Stein, N. CHAINSAW: a program for mutating pdb files used as templates in molecular replacement, J. Appl. Crystallogr. 41, 641-643 (2008).
    • (2008) J. Appl. Crystallogr. , vol.41
    • Stein, N.1
  • 51
    • 3543012707 scopus 로고    scopus 로고
    • Crystallography & NMR system: A new software suite for macromolecular structure determination
    • Brunger, A. T. et al. Crystallography & NMR system: A new software suite for macromolecular structure determination, Acta Crystallogr. D 54, 905-921 (1998).
    • (1998) Acta Crystallogr. D , vol.54
    • Brunger, A.T.1
  • 52
    • 3242886389 scopus 로고    scopus 로고
    • Molprobity: Structure validation and all-atom contact analysis for nucleic acids and their complexes
    • Davis, I. W., Murray, L. W., Richardson, J. S. & Richardson, D. C. MOLPROBITY: structure validation and all-atom contact analysis for nucleic acids and their complexes, Nucleic Acids Res. 32, W615-W619 (2004).
    • (2004) Nucleic Acids Res. , vol.32
    • Davis, I.W.1    Murray, L.W.2    Richardson, J.S.3    Richardson, D.C.4
  • 53
    • 23144448512 scopus 로고    scopus 로고
    • ConSurf 2005: The projection of evolutionary conservation scores of residues on protein structures
    • Landau, M. et al. ConSurf 2005: the projection of evolutionary conservation scores of residues on protein structures. Nucleic Acids Res. 33, W299-W302 (2005).
    • (2005) Nucleic Acids Res. , vol.33
    • Landau, M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.