메뉴 건너뛰기




Volumn 15, Issue 5, 2007, Pages 577-586

Structural Basis for Dynamic Interdomain Movement and RNA Recognition of the Selenocysteine-Specific Elongation Factor SelB

Author keywords

RNA

Indexed keywords

ELONGATION FACTOR; ELONGATION FACTOR TU; GUANOSINE TRIPHOSPHATE; MESSENGER RNA; SELENOCYSTEINE; TRANSFER RNA;

EID: 34248181181     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.str.2007.03.007     Document Type: Article
Times cited : (17)

References (34)
  • 1
    • 0027151982 scopus 로고
    • Interaction of translation factor SELB with the formate dehydrogenase H selenopolypeptide mRNA
    • Baron C., Heider J., and Bock A. Interaction of translation factor SELB with the formate dehydrogenase H selenopolypeptide mRNA. Proc. Natl. Acad. Sci. USA 90 (1993) 4181-4185
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 4181-4185
    • Baron, C.1    Heider, J.2    Bock, A.3
  • 4
    • 0031225689 scopus 로고    scopus 로고
    • Domain structure of the selenocysteine-specific translation factor SelB in prokaryotes
    • Böck A., Hilgenfeld R., Tormay P., Wilting R., and Kromayer M. Domain structure of the selenocysteine-specific translation factor SelB in prokaryotes. Biomed. Environ. Sci. 10 (1997) 125-128
    • (1997) Biomed. Environ. Sci. , vol.10 , pp. 125-128
    • Böck, A.1    Hilgenfeld, R.2    Tormay, P.3    Wilting, R.4    Kromayer, M.5
  • 5
    • 0028103275 scopus 로고
    • The CCP4 suite: programs for protein crystallography
    • CCP4 (Collaborative Computational Project, Number 4)
    • CCP4 (Collaborative Computational Project, Number 4). The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D Biol. Crystallogr. 50 (1994) 760-763
    • (1994) Acta Crystallogr. D Biol. Crystallogr. , vol.50 , pp. 760-763
  • 6
    • 34248213715 scopus 로고    scopus 로고
    • DeLano, W.L. (2002). The PyMOL Molecular Graphics System (http://www.pymol.org).
  • 8
    • 0033119938 scopus 로고    scopus 로고
    • Further additions to MolScript version 1.4, including reading and contouring of electron-density maps
    • Esnouf R.M. Further additions to MolScript version 1.4, including reading and contouring of electron-density maps. Acta Crystallogr. D Biol. Crystallogr. 55 (1999) 938-940
    • (1999) Acta Crystallogr. D Biol. Crystallogr. , vol.55 , pp. 938-940
    • Esnouf, R.M.1
  • 9
    • 0034282536 scopus 로고    scopus 로고
    • Characterization of mSelB, a novel mammalian elongation factor for selenoprotein translation
    • Fagegaltier D., Hubert N., Yamada K., Mizutani T., Carbon P., and Krol A. Characterization of mSelB, a novel mammalian elongation factor for selenoprotein translation. EMBO J. 19 (2000) 4796-4805
    • (2000) EMBO J. , vol.19 , pp. 4796-4805
    • Fagegaltier, D.1    Hubert, N.2    Yamada, K.3    Mizutani, T.4    Carbon, P.5    Krol, A.6
  • 10
    • 0024420343 scopus 로고
    • Identification of a novel translation factor necessary for the incorporation of selenocysteine into protein
    • Forchhammer K., Leinfelder W., and Böck A. Identification of a novel translation factor necessary for the incorporation of selenocysteine into protein. Nature 342 (1989) 453-456
    • (1989) Nature , vol.342 , pp. 453-456
    • Forchhammer, K.1    Leinfelder, W.2    Böck, A.3
  • 11
    • 0036435883 scopus 로고    scopus 로고
    • Structure of prokaryotic SECIS mRNA hairpin and its interaction with elongation factor SelB
    • Fourmy D., Guittet E., and Yoshizawa S. Structure of prokaryotic SECIS mRNA hairpin and its interaction with elongation factor SelB. J. Mol. Biol. 324 (2002) 137-150
    • (2002) J. Mol. Biol. , vol.324 , pp. 137-150
    • Fourmy, D.1    Guittet, E.2    Yoshizawa, S.3
  • 12
    • 0026739536 scopus 로고
    • Coding from a distance: dissection of the mRNA determinants required for the incorporation of selenocysteine into protein
    • Heider J., Baron C., and Bock A. Coding from a distance: dissection of the mRNA determinants required for the incorporation of selenocysteine into protein. EMBO J. 11 (1992) 3759-3766
    • (1992) EMBO J. , vol.11 , pp. 3759-3766
    • Heider, J.1    Baron, C.2    Bock, A.3
  • 14
    • 0040710139 scopus 로고    scopus 로고
    • Selenocysteine inserting RNA elements modulate GTP hydrolysis of elongation factor SelB
    • Hüttenhofer A., and Böck A. Selenocysteine inserting RNA elements modulate GTP hydrolysis of elongation factor SelB. Biochemistry 37 (1998) 885-890
    • (1998) Biochemistry , vol.37 , pp. 885-890
    • Hüttenhofer, A.1    Böck, A.2
  • 15
    • 0029846259 scopus 로고    scopus 로고
    • Solution structure of mRNA hairpins promoting selenocysteine incorporation in Escherichia coli and their base-specific interaction with special elongation factor SELB
    • Hüttenhofer A., Westhof E., and Böck A. Solution structure of mRNA hairpins promoting selenocysteine incorporation in Escherichia coli and their base-specific interaction with special elongation factor SELB. RNA 2 (1996) 354-366
    • (1996) RNA , vol.2 , pp. 354-366
    • Hüttenhofer, A.1    Westhof, E.2    Böck, A.3
  • 16
    • 0026244229 scopus 로고
    • MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures
    • Kraulis P.J. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Cryst. 24 (1991) 946-950
    • (1991) J. Appl. Cryst. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 17
    • 0030568977 scopus 로고    scopus 로고
    • Domain structure of the prokaryotic selenocysteine-specific elongation factor SelB
    • Kromayer M., Wilting R., Tormay P., and Böck A. Domain structure of the prokaryotic selenocysteine-specific elongation factor SelB. J. Mol. Biol. 262 (1996) 413-420
    • (1996) J. Mol. Biol. , vol.262 , pp. 413-420
    • Kromayer, M.1    Wilting, R.2    Tormay, P.3    Böck, A.4
  • 18
    • 0033376119 scopus 로고    scopus 로고
    • Genetic probing of the interaction between the translation factor SelB and its mRNA binding element in Escherichia coli
    • Kromayer M., Neuhierl B., Friebel A., and Bock A. Genetic probing of the interaction between the translation factor SelB and its mRNA binding element in Escherichia coli. Mol. Gen. Genet. 262 (1999) 800-806
    • (1999) Mol. Gen. Genet. , vol.262 , pp. 800-806
    • Kromayer, M.1    Neuhierl, B.2    Friebel, A.3    Bock, A.4
  • 19
    • 13244277554 scopus 로고    scopus 로고
    • Selenocysteine tRNA-specific elongation factor SelB is a structural chimaera of elongation and initiation factors
    • Leibundgut M., Frick C., Thanbichler M., Bock A., and Ban N. Selenocysteine tRNA-specific elongation factor SelB is a structural chimaera of elongation and initiation factors. EMBO J. 24 (2005) 11-22
    • (2005) EMBO J. , vol.24 , pp. 11-22
    • Leibundgut, M.1    Frick, C.2    Thanbichler, M.3    Bock, A.4    Ban, N.5
  • 20
    • 0033764922 scopus 로고    scopus 로고
    • The bulged nucleotide in the Escherichia coli minimal selenocysteine insertion sequence participates in interaction with SelB: a genetic approach
    • Li C., Reches M., and Engelberg-Kulka H. The bulged nucleotide in the Escherichia coli minimal selenocysteine insertion sequence participates in interaction with SelB: a genetic approach. J. Bacteriol. 182 (2000) 6302-6307
    • (2000) J. Bacteriol. , vol.182 , pp. 6302-6307
    • Li, C.1    Reches, M.2    Engelberg-Kulka, H.3
  • 21
    • 0026319199 scopus 로고
    • Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls A., Sharp K.A., and Honig B. Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins 11 (1991) 281-296
    • (1991) Proteins , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3
  • 22
    • 0037184536 scopus 로고    scopus 로고
    • Selection of tRNA by the ribosome requires a transition from an open to a closed form
    • Ogle J.M., Murphy F.V., Tarry M.J., and Ramakrishnan V. Selection of tRNA by the ribosome requires a transition from an open to a closed form. Cell 111 (2002) 721-732
    • (2002) Cell , vol.111 , pp. 721-732
    • Ogle, J.M.1    Murphy, F.V.2    Tarry, M.J.3    Ramakrishnan, V.4
  • 23
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Carter Jr. C.W., and Sweet R.M. (Eds), Academic Press, New York
    • Otwinowski Z., and Minor W. Processing of X-ray diffraction data collected in oscillation mode. In: Carter Jr. C.W., and Sweet R.M. (Eds). Methods in Enzymology (1997), Academic Press, New York 307-326
    • (1997) Methods in Enzymology , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 24
    • 0033168212 scopus 로고    scopus 로고
    • Induced fit in initial selection and proofreading of aminoacyl-tRNA on the ribosome
    • Pape T., Wintermeyer W., and Rodnina M. Induced fit in initial selection and proofreading of aminoacyl-tRNA on the ribosome. EMBO J. 18 (1999) 3800-3807
    • (1999) EMBO J. , vol.18 , pp. 3800-3807
    • Pape, T.1    Wintermeyer, W.2    Rodnina, M.3
  • 25
    • 33646488074 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray analysis of the mRNA-binding domain of elongation factor selB in complex with RNA
    • Rasubala L., Fourmy D., Ose T., Kohda D., Maenaka K., and Yoshizawa S. Crystallization and preliminary X-ray analysis of the mRNA-binding domain of elongation factor selB in complex with RNA. Acta Crystallogr. F61 (2005) 296-298
    • (2005) Acta Crystallogr. , vol.F61 , pp. 296-298
    • Rasubala, L.1    Fourmy, D.2    Ose, T.3    Kohda, D.4    Maenaka, K.5    Yoshizawa, S.6
  • 26
    • 0035015556 scopus 로고    scopus 로고
    • Heterologous expression of archaeal selenoprotein genes directed by the SECIS element located in the 3′ non-translated region
    • Rother M., Resch A., Gardner W.L., Whitman W.B., and Bock A. Heterologous expression of archaeal selenoprotein genes directed by the SECIS element located in the 3′ non-translated region. Mol. Microbiol. 40 (2001) 900-908
    • (2001) Mol. Microbiol. , vol.40 , pp. 900-908
    • Rother, M.1    Resch, A.2    Gardner, W.L.3    Whitman, W.B.4    Bock, A.5
  • 27
    • 0038813923 scopus 로고    scopus 로고
    • Revised Escherichia coli selenocysteine insertion requirements determined by in vivo screening of combinatorial libraries of SECIS variants
    • Sandman K.E., Tardiff D.F., Neely L.A., and Noren C.J. Revised Escherichia coli selenocysteine insertion requirements determined by in vivo screening of combinatorial libraries of SECIS variants. Nucleic Acids Res. 31 (2003) 2234-2241
    • (2003) Nucleic Acids Res. , vol.31 , pp. 2234-2241
    • Sandman, K.E.1    Tardiff, D.F.2    Neely, L.A.3    Noren, C.J.4
  • 28
    • 0036682596 scopus 로고    scopus 로고
    • Crystal structure of an mRNA-binding fragment of Moorella thermoacetica elongation factor SelB
    • Selmer M., and Su X.D. Crystal structure of an mRNA-binding fragment of Moorella thermoacetica elongation factor SelB. EMBO J. 21 (2002) 4145-4153
    • (2002) EMBO J. , vol.21 , pp. 4145-4153
    • Selmer, M.1    Su, X.D.2
  • 30
    • 0039765528 scopus 로고    scopus 로고
    • Kinetics of the interaction of translation factor SelB from Escherichia coli with guanosine nucleotides and selenocysteine insertion sequence RNA
    • Thanbichler M., Bock A., and Goody R.S. Kinetics of the interaction of translation factor SelB from Escherichia coli with guanosine nucleotides and selenocysteine insertion sequence RNA. J. Biol. Chem. 275 (2000) 20458-20466
    • (2000) J. Biol. Chem. , vol.275 , pp. 20458-20466
    • Thanbichler, M.1    Bock, A.2    Goody, R.S.3
  • 32
    • 0035182073 scopus 로고    scopus 로고
    • Use of TLS parameters to model anisotropic displacements in macromolecular refinement
    • Winn M., Isupov M., and Murshudov G.N. Use of TLS parameters to model anisotropic displacements in macromolecular refinement. Acta Crystallogr. D Biol. Crystallogr. 57 (2001) 122-133
    • (2001) Acta Crystallogr. D Biol. Crystallogr. , vol.57 , pp. 122-133
    • Winn, M.1    Isupov, M.2    Murshudov, G.N.3
  • 33
    • 33644872571 scopus 로고    scopus 로고
    • LAFIRE: software for automating the refinement process of protein-structure analysis
    • Yao M., Zhou Y., and Tanaka I. LAFIRE: software for automating the refinement process of protein-structure analysis. Acta Crystallogr. D Biol. Crystallogr. 62 (2006) 189-196
    • (2006) Acta Crystallogr. D Biol. Crystallogr. , vol.62 , pp. 189-196
    • Yao, M.1    Zhou, Y.2    Tanaka, I.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.