메뉴 건너뛰기




Volumn 9, Issue 1, 2003, Pages 100-111

Mechanism of molecular interactions for tRNAVal recognition by valyl-tRNA synthetase

Author keywords

Aminoacyl tRNA synthetase; RNA protein interaction; Translation; tRNA; X ray crystallography

Indexed keywords

AMINO ACID TRANSFER RNA LIGASE; VALINE TRANSFER RNA; VALINE TRANSFER RNA LIGASE;

EID: 0037273353     PISSN: 13558382     EISSN: None     Source Type: Journal    
DOI: 10.1261/rna.2760703     Document Type: Article
Times cited : (60)

References (45)
  • 2
  • 3
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project No. 4. 1994. The CCP4 suite: Programs for protein crystallography. Acta Crystallogr. D50: 760-763.
    • (1994) Acta Crystallogr. , vol.D50 , pp. 760-763
  • 4
    • 0034612210 scopus 로고    scopus 로고
    • CP1 domain in Escherichia coli leucyl-tRNA synthetase is crucial for its editing function
    • Chen, J.F., Guo, N.N., Li, T., Wang, E.D., and Wang, Y.L. 2000. CP1 domain in Escherichia coli leucyl-tRNA synthetase is crucial for its editing function. Biochemistry 39: 6726-6731.
    • (2000) Biochemistry , vol.39 , pp. 6726-6731
    • Chen, J.F.1    Guo, N.N.2    Li, T.3    Wang, E.D.4    Wang, Y.L.5
  • 5
    • 0025804403 scopus 로고
    • Recognition of Escherichia coli valine transfer RNA by its cognate synthetase: A fluorine-19 NMR study
    • Chu, W.C. and Horowitz, J. 1991. Recognition of Escherichia coli valine transfer RNA by its cognate synthetase: A fluorine-19 NMR study. Biochemistry 30: 1655-1663.
    • (1991) Biochemistry , vol.30 , pp. 1655-1663
    • Chu, W.C.1    Horowitz, J.2
  • 6
    • 0026468016 scopus 로고
    • Fluorine-19 nuclear magnetic resonance as a probe of the solution structure of mutants of 5-fluorouracil-substituted Escherichia coli valine tRNA
    • Chu, W.C., Feiz, V., Derrick, W.B., and Horowitz, J. 1992. Fluorine-19 nuclear magnetic resonance as a probe of the solution structure of mutants of 5-fluorouracil-substituted Escherichia coli valine tRNA. J. Mol. Biol. 227: 1164-1172.
    • (1992) J. Mol. Biol. , vol.227 , pp. 1164-1172
    • Chu, W.C.1    Feiz, V.2    Derrick, W.B.3    Horowitz, J.4
  • 7
    • 0029099218 scopus 로고
    • Eleven down and nine to go
    • Cusack, S. 1995. Eleven down and nine to go. Nat. Struct. Biol. 2: 824-831.
    • (1995) Nat. Struct. Biol. , vol.2 , pp. 824-831
    • Cusack, S.1
  • 8
    • 0034657687 scopus 로고    scopus 로고
    • The 2 Å crystal structure of leucyl-tRNA synthetase and its complex with a leucyladenylate analogue
    • Cusack, S., Yaremchuk, A., and Tukalo, M. 2000. The 2 Å crystal structure of leucyl-tRNA synthetase and its complex with a leucyladenylate analogue. EMBO J. 19: 2351-2361.
    • (2000) EMBO J. , vol.19 , pp. 2351-2361
    • Cusack, S.1    Yaremchuk, A.2    Tukalo, M.3
  • 9
    • 0034332436 scopus 로고    scopus 로고
    • tRNA aminoacylation by arginyl-tRNA synthetase: Induced conformations during substrates binding
    • Delagoutte, B., Moras, D., and Cavarelli, J. 2000. tRNA aminoacylation by arginyl-tRNA synthetase: Induced conformations during substrates binding. EMBO J. 19: 5599-5610.
    • (2000) EMBO J. , vol.19 , pp. 5599-5610
    • Delagoutte, B.1    Moras, D.2    Cavarelli, J.3
  • 10
    • 0027674975 scopus 로고
    • The aminoacyl-tRNA synthetase family: Modules at work
    • Delarue, M. and Moras, D. 1993. The aminoacyl-tRNA synthetase family: Modules at work. Bioessays 15: 675-687.
    • (1993) Bioessays , vol.15 , pp. 675-687
    • Delarue, M.1    Moras, D.2
  • 11
    • 0027370662 scopus 로고
    • Probing structural differences between native and in vitro transcribed Escherichia coli valine transfer RNA: Evidence for stable base modification-dependent conformers
    • Derrick, W. B. and Horrowitz, J. 1993. Probing structural differences between native and in vitro transcribed Escherichia coli valine transfer RNA: Evidence for stable base modification-dependent conformers. Nucleic Acids Res. BO21: 948-53.
    • (1993) Nucleic Acids Res. , vol.BO21 , pp. 948-953
    • Derrick, W.B.1    Horrowitz, J.2
  • 12
    • 0025158208 scopus 로고
    • Partition of tRNA synthetases into two classes based on mutually exclusive sets of sequence motifs
    • Eriani, G., Delarue, M., Poch, O., Gangloff, J., Moras, D. 1990. Partition of tRNA synthetases into two classes based on mutually exclusive sets of sequence motifs. Nature 347: 203-206.
    • (1990) Nature , vol.347 , pp. 203-206
    • Eriani, G.1    Delarue, M.2    Poch, O.3    Gangloff, J.4    Moras, D.5
  • 13
    • 0017230165 scopus 로고
    • Mechanism of aminoacylation of tRNA. Proof of the aminoacyl adenylate pathway for the isoleucyl- and tyrosyl-tRNA synthetases from Escherichia coli K12
    • Fersht, A.R. and Kaethner, M.M. 1976. Mechanism of aminoacylation of tRNA. Proof of the aminoacyl adenylate pathway for the isoleucyl- and tyrosyl-tRNA synthetases from Escherichia coli K12. Biochemistry 15: 818-823.
    • (1976) Biochemistry , vol.15 , pp. 818-823
    • Fersht, A.R.1    Kaethner, M.M.2
  • 15
    • 3643114575 scopus 로고    scopus 로고
    • Universal rules and idiosyncratic features in tRNA identity
    • Giegè, R., Sissler, M., and Florentz, C. 1998. Universal rules and idiosyncratic features in tRNA identity. Nucleic Acids Res. 26: 5017-5035.
    • (1998) Nucleic Acids Res. , vol.26 , pp. 5017-5035
    • Giegè, R.1    Sissler, M.2    Florentz, C.3
  • 16
    • 0033564663 scopus 로고    scopus 로고
    • Synthetase recognition determinants of E. coli valine transfer RNA
    • Horowitz, J., Chu, W.C., Derrick, W.B., Liu, J.C., Liu, M., and Yue, D. 1999. Synthetase recognition determinants of E. coli valine transfer RNA. Biochemistry 38: 7737-7746.
    • (1999) Biochemistry , vol.38 , pp. 7737-7746
    • Horowitz, J.1    Chu, W.C.2    Derrick, W.B.3    Liu, J.C.4    Liu, M.5    Yue, D.6
  • 17
    • 84889120137 scopus 로고
    • Improved methods for binding protein models in electron density maps and the location of errors in these models
    • Jones, T.A., Zou, J.Y., Cowan, S.W., and Kjeldgaard, M. 1991. Improved methods for binding protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A47: 110-119.
    • (1991) Acta Crystallogr. , vol.A47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 18
    • 0035210865 scopus 로고    scopus 로고
    • Shifted positioning of the anticodon nucleotide residues of amber suppressor tRNA species by Escherichia coli arginyl-tRNA synthetase
    • Kiga, D., Sakamoto, K., Sato, S., Hirao, I., and Yokoyama, S. 2001. Shifted positioning of the anticodon nucleotide residues of amber suppressor tRNA species by Escherichia coli arginyl-tRNA synthetase. Eur. J. Biochem. 268: 6207-6213.
    • (2001) Eur. J. Biochem. , vol.268 , pp. 6207-6213
    • Kiga, D.1    Sakamoto, K.2    Sato, S.3    Hirao, I.4    Yokoyama, S.5
  • 19
    • 0029365773 scopus 로고
    • Cell-free synthesis and amino acid-selective stable isotope labeling of proteins for NMR analysis
    • Kigawa, T., Muto, Y., and Yokoyama, S. 1995. Cell-free synthesis and amino acid-selective stable isotope labeling of proteins for NMR analysis. J. Biomol. NMR 6:129-134.
    • (1995) J. Biomol. NMR , vol.6 , pp. 129-134
    • Kigawa, T.1    Muto, Y.2    Yokoyama, S.3
  • 20
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • Koradi, R., Billeter, M., and Wüthrich, K. 1996. MOLMOL: A program for display and analysis of macromolecular structures. J. Mol. Graph. 14: 51-55.
    • (1996) J. Mol. Graph. , vol.14 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wüthrich, K.3
  • 21
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P.J. 1991. MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallog. 24: 946-950.
    • (1991) J. Appl. Crystallog. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 22
    • 0029854940 scopus 로고    scopus 로고
    • Aminoacylation error correction
    • Lin, L., Hale, S.P., and Schimmel, P. 1996. Aminoacylation error correction. Nature 384: 33-34.
    • (1996) Nature , vol.384 , pp. 33-34
    • Lin, L.1    Hale, S.P.2    Schimmel, P.3
  • 23
    • 0024300362 scopus 로고
    • Changing the acceptor identity of a transfer RNA by altering nucleotides in a "variable pocket"
    • McClain, W.H. and Foss, K. 1988. Changing the acceptor identity of a transfer RNA by altering nucleotides in a "variable pocket". Science 241: 1804-1807.
    • (1988) Science , vol.241 , pp. 1804-1807
    • McClain, W.H.1    Foss, K.2
  • 25
    • 0030815133 scopus 로고    scopus 로고
    • Raster3D: Photorealistic molecular graphics
    • Merritt, E.A. and Bacon, D.J. 1997. Raster3D: Photorealistic molecular graphics. Methods Enzymol. 277: 505-524.
    • (1997) Methods Enzymol. , vol.277 , pp. 505-524
    • Merritt, E.A.1    Bacon, D.J.2
  • 26
    • 0023734317 scopus 로고
    • Codon and amino-acid specificities of a transfer RNA are both converted by a single post-transcriptional modification
    • Muramatsu, T., Nishikawa, K., Nemoto, F., Kuchino, Y., Nishimura, S., Miyazawa, T., and Yokoyama, S. 1988. Codon and amino-acid specificities of a transfer RNA are both converted by a single post-transcriptional modification. Nature 336: 179-181.
    • (1988) Nature , vol.336 , pp. 179-181
    • Muramatsu, T.1    Nishikawa, K.2    Nemoto, F.3    Kuchino, Y.4    Nishimura, S.5    Miyazawa, T.6    Yokoyama, S.7
  • 28
    • 84920325457 scopus 로고
    • AMoRe: An automated package for molecular replacement
    • Navaza, J. 1994. AMoRe: An automated package for molecular replacement. Acta Crystallogr. A50: 157-163.
    • (1994) Acta Crystallogr. , vol.A50 , pp. 157-163
    • Navaza, J.1
  • 29
    • 0037013921 scopus 로고    scopus 로고
    • Structural origins of amino acid selection without editing by cysteinyl-tRNA synthetase
    • Newberry, K. J., Hou, Y.-M., and Perona, J. 2002. Structural origins of amino acid selection without editing by cysteinyl-tRNA synthetase. EMBO J. 21: 2778-2787.
    • (2002) EMBO J. , vol.21 , pp. 2778-2787
    • Newberry, K.J.1    Hou, Y.-M.2    Perona, J.3
  • 30
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls, A., Sharp, K.A., and Honig, B. 1991. Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins 11: 281-296.
    • (1991) Proteins , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3
  • 31
    • 0028266202 scopus 로고
    • Molecular recognition of the identity-determinant set of isoleucine transfer RNA from Escherichia coli
    • Nureki, O., Niimi, T., Muramatsu, T., Kanno, H., Kohno, T., Florentz, C., Giegé, R., and Yokoyama, S. 1994. Molecular recognition of the identity-determinant set of isoleucine transfer RNA from Escherichia coli. J. Mol. Biol. 236: 710-724.
    • (1994) J. Mol. Biol. , vol.236 , pp. 710-724
    • Nureki, O.1    Niimi, T.2    Muramatsu, T.3    Kanno, H.4    Kohno, T.5    Florentz, C.6    Giegé, R.7    Yokoyama, S.8
  • 33
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z. and Minor, W. 1997. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276: 307-326.
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 34
    • 0025735619 scopus 로고
    • Anticodon-dependent aminoacylation of a noncognate tRNA with isoleucine, valine, and phenylalanine in vivo
    • Pallanck, L. and Schulman, L.H. 1991. Anticodon-dependent aminoacylation of a noncognate tRNA with isoleucine, valine, and phenylalanine in vivo. Proc. Natl. Acad. Sci. 88: 3872-3876.
    • (1991) Proc. Natl. Acad. Sci. , vol.88 , pp. 3872-3876
    • Pallanck, L.1    Schulman, L.H.2
  • 36
    • 0025744320 scopus 로고
    • Structural basis of anticodon loop recognition by glutaminyl-tRNA synthetase
    • Rould, M.A., Perona, J.J., and Steitz, T.A. 1991. Structural basis of anticodon loop recognition by glutaminyl-tRNA synthetase. Nature 352: 213-218.
    • (1991) Nature , vol.352 , pp. 213-218
    • Rould, M.A.1    Perona, J.J.2    Steitz, T.A.3
  • 37
    • 0017658685 scopus 로고
    • Structural requirements for aminoacylation of Escherichia coli formylmethionine transfer RNA
    • Schulman, L.H. and Pelka, H. 1977. Structural requirements for aminoacylation of Escherichia coli formylmethionine transfer RNA. Biochemistry 16: 4256-4265.
    • (1977) Biochemistry , vol.16 , pp. 4256-4265
    • Schulman, L.H.1    Pelka, H.2
  • 38
    • 0035119935 scopus 로고    scopus 로고
    • Structural basis for anticodon recognition by discriminating glutamyl- tRNA synthetase
    • Sekine, S., Nureki, O., Shimada, A., Vassylyev, D.G., and Yokoyama, S. 2001. Structural basis for anticodon recognition by discriminating glutamyl- tRNA synthetase. Nat. Struct. Biol. 8: 203-206.
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 203-206
    • Sekine, S.1    Nureki, O.2    Shimada, A.3    Vassylyev, D.G.4    Yokoyama, S.5
  • 39
    • 0013200222 scopus 로고    scopus 로고
    • Structural and mutational studies of the recognition of the arginine tRNA-specific major identity element, A20, by arginyl-tRNA synthetase
    • Shimada, A., Nureki, O., Goto, M., Takahashi, S., and Yokoyama, S. 2001. Structural and mutational studies of the recognition of the arginine tRNA-specific major identity element, A20, by arginyl-tRNA synthetase. Proc. Natl. Acad. Sci. 6: 6.
    • (2001) Proc. Natl. Acad. Sci. , vol.6 , pp. 6
    • Shimada, A.1    Nureki, O.2    Goto, M.3    Takahashi, S.4    Yokoyama, S.5
  • 43
    • 0017194883 scopus 로고
    • Three-dimensional structure of a transfer RNA in two crystal forms
    • Sussman, J.L. and Kim, S. 1976 Three-dimensional structure of a transfer RNA in two crystal forms. Science 192: 853-858.
    • (1976) Science , vol.192 , pp. 853-858
    • Sussman, J.L.1    Kim, S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.