메뉴 건너뛰기




Volumn 1804, Issue 1, 2010, Pages 147-155

The N-terminal region is crucial for the thermostability of the G-domain of Bacillus stearothermophilus EF-Tu

Author keywords

Bacillus; EF Tu; G protein; G domain; Thermostability

Indexed keywords

ELONGATION FACTOR TU; GUANINE NUCLEOTIDE BINDING PROTEIN;

EID: 71649106884     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2009.09.024     Document Type: Article
Times cited : (5)

References (37)
  • 2
    • 0029958571 scopus 로고    scopus 로고
    • The GTP binding motif: variations on a theme.
    • Kjeldgaard M., Nyborg J., and Clark B.F. The GTP binding motif: variations on a theme. FASEB J. 10 (1996) 1347-1368
    • (1996) FASEB J. , vol.10 , pp. 1347-1368
    • Kjeldgaard, M.1    Nyborg, J.2    Clark, B.F.3
  • 4
    • 0027179878 scopus 로고
    • Crystal structure of active elongation factor Tu reveals major domain rearrangements [published erratum appears in Nature 1993 Sep 23;365(6444):368]
    • Berchtold H., Reshetnikova L., Reiser C.O., Schirmer N.K., Sprinzl M., and Hilgenfeld R. Crystal structure of active elongation factor Tu reveals major domain rearrangements [published erratum appears in Nature 1993 Sep 23;365(6444):368]. Nature 365 (1993) 126-132
    • (1993) Nature , vol.365 , pp. 126-132
    • Berchtold, H.1    Reshetnikova, L.2    Reiser, C.O.3    Schirmer, N.K.4    Sprinzl, M.5    Hilgenfeld, R.6
  • 5
    • 0033593370 scopus 로고    scopus 로고
    • Crystal structure of intact elongation factor EF-Tu from Escherichia coli in GDP conformation at 2.05 A resolution.
    • Song H., Parsons M.R., Rowsell S., Leonard G., and Phillips S.E. Crystal structure of intact elongation factor EF-Tu from Escherichia coli in GDP conformation at 2.05 A resolution. J. Mol. Biol. 285 (1999) 1245-1256
    • (1999) J. Mol. Biol. , vol.285 , pp. 1245-1256
    • Song, H.1    Parsons, M.R.2    Rowsell, S.3    Leonard, G.4    Phillips, S.E.5
  • 6
    • 0346733334 scopus 로고    scopus 로고
    • Thermostability of multidomain proteins: elongation factors EF-Tu from Escherichia coli and Bacillus stearothermophilus and their chimeric forms
    • Sanderova H., Hulkova M., Malon P., Kepkova M., and Jonak J. Thermostability of multidomain proteins: elongation factors EF-Tu from Escherichia coli and Bacillus stearothermophilus and their chimeric forms. Protein Sci. 13 (2004) 89-99
    • (2004) Protein Sci. , vol.13 , pp. 89-99
    • Sanderova, H.1    Hulkova, M.2    Malon, P.3    Kepkova, M.4    Jonak, J.5
  • 7
    • 23944466341 scopus 로고    scopus 로고
    • Opposite roles of domains 2 + 3 of Escherichia coli EF-Tu and Bacillus stearothermophilus EF-Tu in the regulation of EF-Tu GTPase activity
    • Sanderova H., and Jonak J. Opposite roles of domains 2 + 3 of Escherichia coli EF-Tu and Bacillus stearothermophilus EF-Tu in the regulation of EF-Tu GTPase activity. Biochim. Biophys. Acta 1752 (2005) 11-17
    • (2005) Biochim. Biophys. Acta , vol.1752 , pp. 11-17
    • Sanderova, H.1    Jonak, J.2
  • 8
    • 0030587932 scopus 로고    scopus 로고
    • An alpha to beta conformational switch in EF-Tu.
    • Abel K., Yoder M.D., Hilgenfeld R., and Jurnak F. An alpha to beta conformational switch in EF-Tu. Structure 4 (1996) 1153-1159
    • (1996) Structure , vol.4 , pp. 1153-1159
    • Abel, K.1    Yoder, M.D.2    Hilgenfeld, R.3    Jurnak, F.4
  • 9
    • 0035933781 scopus 로고    scopus 로고
    • The importance of structural transitions of the switch II region for the functions of elongation factor Tu on the ribosome
    • Knudsen C., Wieden H.J., and Rodnina M.V. The importance of structural transitions of the switch II region for the functions of elongation factor Tu on the ribosome. J. Biol. Chem. 276 (2001) 22183-22190
    • (2001) J. Biol. Chem. , vol.276 , pp. 22183-22190
    • Knudsen, C.1    Wieden, H.J.2    Rodnina, M.V.3
  • 10
    • 0037133662 scopus 로고    scopus 로고
    • The tRNA specificity of Thermus thermophilus EF-Tu
    • Asahara H., and Uhlenbeck O.C. The tRNA specificity of Thermus thermophilus EF-Tu. Proc. Natl. Acad. Sci. U. S. A 99 (2002) 3499-3504
    • (2002) Proc. Natl. Acad. Sci. U. S. A , vol.99 , pp. 3499-3504
    • Asahara, H.1    Uhlenbeck, O.C.2
  • 11
    • 43049157544 scopus 로고    scopus 로고
    • Structural studies of elongation and release factors
    • Noble C.G., and Song H. Structural studies of elongation and release factors. Cell Mol. Life Sci. 65 (2008) 1335-1346
    • (2008) Cell Mol. Life Sci. , vol.65 , pp. 1335-1346
    • Noble, C.G.1    Song, H.2
  • 12
    • 59049095244 scopus 로고    scopus 로고
    • Visualizing the protein synthesis machinery: new focus on the translational GTPase elongation factor Tu
    • Rodnina M.V. Visualizing the protein synthesis machinery: new focus on the translational GTPase elongation factor Tu. Proc. Natl. Acad. Sci. U. S. A 106 (2009) 969-970
    • (2009) Proc. Natl. Acad. Sci. U. S. A , vol.106 , pp. 969-970
    • Rodnina, M.V.1
  • 14
    • 33744925655 scopus 로고    scopus 로고
    • Explanation of the stability of thermophilic proteins based on unique micromorphology
    • Melchionna S., Sinibaldi R., and Briganti G. Explanation of the stability of thermophilic proteins based on unique micromorphology. Biophys. J. 90 (2006) 4204-4212
    • (2006) Biophys. J. , vol.90 , pp. 4204-4212
    • Melchionna, S.1    Sinibaldi, R.2    Briganti, G.3
  • 15
    • 38149111171 scopus 로고    scopus 로고
    • Differences in amino acids composition and coupling patterns between mesophilic and thermophilic proteins
    • Zhou X.X., Wang Y.B., Pan Y.J., and Li W.F. Differences in amino acids composition and coupling patterns between mesophilic and thermophilic proteins. Amino Acids 34 (2008) 25-33
    • (2008) Amino Acids , vol.34 , pp. 25-33
    • Zhou, X.X.1    Wang, Y.B.2    Pan, Y.J.3    Li, W.F.4
  • 17
    • 34047184287 scopus 로고    scopus 로고
    • Bacterial elongation factors EF-Tu, their mutants, chimeric forms, and domains: isolation and purification
    • Jonak J. Bacterial elongation factors EF-Tu, their mutants, chimeric forms, and domains: isolation and purification. J. Chromatogr. B Analyt. Technol. Biomed. Life Sci. 849 (2007) 141-153
    • (2007) J. Chromatogr. B Analyt. Technol. Biomed. Life Sci. , vol.849 , pp. 141-153
    • Jonak, J.1
  • 18
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 21
    • 0025117682 scopus 로고
    • Complete nucleotide sequences of seven eubacterial genes coding for the elongation factor Tu: functional, structural and phylogenetic evaluations
    • Ludwig W., Weizenegger M., Betzl D., Leidel E., Lenz T., Ludvigsen A., Mollenhoff D., Wenzig P., and Schleifer K.H. Complete nucleotide sequences of seven eubacterial genes coding for the elongation factor Tu: functional, structural and phylogenetic evaluations. Arch. Microbiol. 153 (1990) 241-247
    • (1990) Arch. Microbiol. , vol.153 , pp. 241-247
    • Ludwig, W.1    Weizenegger, M.2    Betzl, D.3    Leidel, E.4    Lenz, T.5    Ludvigsen, A.6    Mollenhoff, D.7    Wenzig, P.8    Schleifer, K.H.9
  • 22
    • 0034693042 scopus 로고    scopus 로고
    • Structural and genomic correlates of hyperthermostability
    • Cambillau C., and Claverie J.M. Structural and genomic correlates of hyperthermostability. J. Biol. Chem. 275 (2000) 32383-32386
    • (2000) J. Biol. Chem. , vol.275 , pp. 32383-32386
    • Cambillau, C.1    Claverie, J.M.2
  • 23
    • 0037931826 scopus 로고    scopus 로고
    • Genomic correlates of hyperthermostability, an update
    • Suhre K., and Claverie J.M. Genomic correlates of hyperthermostability, an update. J. Biol. Chem. 278 (2003) 17198-17202
    • (2003) J. Biol. Chem. , vol.278 , pp. 17198-17202
    • Suhre, K.1    Claverie, J.M.2
  • 25
    • 0031591389 scopus 로고    scopus 로고
    • The refined crystal structure of Bacillus cereus oligo-1,6-glucosidase at 2.0 A resolution: structural characterization of proline-substitution sites for protein thermostabilization
    • Watanabe K., Hata Y., Kizaki H., Katsube Y., and Suzuki Y. The refined crystal structure of Bacillus cereus oligo-1,6-glucosidase at 2.0 A resolution: structural characterization of proline-substitution sites for protein thermostabilization. J. Mol. Biol. 269 (1997) 142-153
    • (1997) J. Mol. Biol. , vol.269 , pp. 142-153
    • Watanabe, K.1    Hata, Y.2    Kizaki, H.3    Katsube, Y.4    Suzuki, Y.5
  • 26
    • 0032548923 scopus 로고    scopus 로고
    • Investigation of functional aspects of the N-terminal region of elongation factor Tu from Escherichia coli using a protein engineering approach
    • Laurberg M., Mansilla F., Clark B.F., and Knudsen C.R. Investigation of functional aspects of the N-terminal region of elongation factor Tu from Escherichia coli using a protein engineering approach. J. Biol. Chem. 273 (1998) 4387-4391
    • (1998) J. Biol. Chem. , vol.273 , pp. 4387-4391
    • Laurberg, M.1    Mansilla, F.2    Clark, B.F.3    Knudsen, C.R.4
  • 27
    • 0030727501 scopus 로고    scopus 로고
    • Mutational analysis of Escherichia coli elongation factor Tu in search of a role for the N-terminal region
    • Mansilla F., Knudsen C.R., Laurberg M., and Clark B.F. Mutational analysis of Escherichia coli elongation factor Tu in search of a role for the N-terminal region. Protein Eng. 10 (1997) 927-934
    • (1997) Protein Eng. , vol.10 , pp. 927-934
    • Mansilla, F.1    Knudsen, C.R.2    Laurberg, M.3    Clark, B.F.4
  • 28
    • 0032537423 scopus 로고    scopus 로고
    • Mutational analysis of Glu272 in elongation factor 1A of E. coli
    • Mansilla F., Knudsen C.R., and Clark B.F. Mutational analysis of Glu272 in elongation factor 1A of E. coli. FEBS Lett. 429 (1998) 417-420
    • (1998) FEBS Lett. , vol.429 , pp. 417-420
    • Mansilla, F.1    Knudsen, C.R.2    Clark, B.F.3
  • 29
    • 0027917990 scopus 로고
    • The crystal structure of elongation factor EF-Tu from Thermus aquaticus in the GTP conformation.
    • Kjeldgaard M., Nissen P., Thirup S., and Nyborg J. The crystal structure of elongation factor EF-Tu from Thermus aquaticus in the GTP conformation. Structure 1 (1993) 35-50
    • (1993) Structure , vol.1 , pp. 35-50
    • Kjeldgaard, M.1    Nissen, P.2    Thirup, S.3    Nyborg, J.4
  • 30
    • 0028812785 scopus 로고
    • Crystal structure of the ternary complex of Phe-tRNAPhe, EF-Tu, and a GTP analog [see comments]
    • Nissen P., Kjeldgaard M., Thirup S., Polekhina G., Reshetnikova L., Clark B.F., and Nyborg J. Crystal structure of the ternary complex of Phe-tRNAPhe, EF-Tu, and a GTP analog [see comments]. Science 270 (1995) 1464-1472
    • (1995) Science , vol.270 , pp. 1464-1472
    • Nissen, P.1    Kjeldgaard, M.2    Thirup, S.3    Polekhina, G.4    Reshetnikova, L.5    Clark, B.F.6    Nyborg, J.7
  • 31
    • 0033081413 scopus 로고    scopus 로고
    • The crystal structure of Cys-tRNACys-EF-Tu-GDPNP reveals general and specific features in the ternary complex and in tRNA.
    • Nissen P., Thirup S., Kjeldgaard M., and Nyborg J. The crystal structure of Cys-tRNACys-EF-Tu-GDPNP reveals general and specific features in the ternary complex and in tRNA. Struct. Fold. Des. 7 (1999) 143-156
    • (1999) Struct. Fold. Des. , vol.7 , pp. 143-156
    • Nissen, P.1    Thirup, S.2    Kjeldgaard, M.3    Nyborg, J.4
  • 32
    • 0030891289 scopus 로고    scopus 로고
    • N-terminal hydrophobic residues of the G-protein ADP-ribosylation factor-1 insert into membrane phospholipids upon GDP to GTP exchange
    • Antonny B., Beraud-Dufour S., Chardin P., and Chabre M. N-terminal hydrophobic residues of the G-protein ADP-ribosylation factor-1 insert into membrane phospholipids upon GDP to GTP exchange. Biochemistry 36 (1997) 4675-4684
    • (1997) Biochemistry , vol.36 , pp. 4675-4684
    • Antonny, B.1    Beraud-Dufour, S.2    Chardin, P.3    Chabre, M.4
  • 33
    • 0028556994 scopus 로고
    • Structure of the human ADP-ribosylation factor 1 complexed with GDP
    • Amor J.C., Harrison D.H., Kahn R.A., and Ringe D. Structure of the human ADP-ribosylation factor 1 complexed with GDP. Nature 372 (1994) 704-708
    • (1994) Nature , vol.372 , pp. 704-708
    • Amor, J.C.1    Harrison, D.H.2    Kahn, R.A.3    Ringe, D.4
  • 34
    • 0035834688 scopus 로고    scopus 로고
    • Structures of yeast ARF2 and ARL1: distinct roles for the N terminus in the structure and function of ARF family GTPases
    • Amor J.C., Horton J.R., Zhu X., Wang Y., Sullards C., Ringe D., Cheng X., and Kahn R.A. Structures of yeast ARF2 and ARL1: distinct roles for the N terminus in the structure and function of ARF family GTPases. J. Biol. Chem. 276 (2001) 42477-42484
    • (2001) J. Biol. Chem. , vol.276 , pp. 42477-42484
    • Amor, J.C.1    Horton, J.R.2    Zhu, X.3    Wang, Y.4    Sullards, C.5    Ringe, D.6    Cheng, X.7    Kahn, R.A.8
  • 36
    • 34247529977 scopus 로고    scopus 로고
    • The N-terminal region of the starch-branching enzyme from Phaseolus vulgaris L. is essential for optimal catalysis and structural stability
    • Hamada S., Ito H., Ueno H., Takeda Y., and Matsui H. The N-terminal region of the starch-branching enzyme from Phaseolus vulgaris L. is essential for optimal catalysis and structural stability. Phytochemistry 68 (2007) 1367-1375
    • (2007) Phytochemistry , vol.68 , pp. 1367-1375
    • Hamada, S.1    Ito, H.2    Ueno, H.3    Takeda, Y.4    Matsui, H.5
  • 37
    • 34247484991 scopus 로고    scopus 로고
    • The N-terminal region is important for the nuclease activity and thermostability of the flap endonuclease-1 from Sulfolobus tokodaii
    • Horie M., Fukui K., Xie M., Kageyama Y., Hamada K., Sakihama Y., Sugimori K., and Matsumoto K. The N-terminal region is important for the nuclease activity and thermostability of the flap endonuclease-1 from Sulfolobus tokodaii. Biosci. Biotechnol. Biochem. 71 (2007) 855-865
    • (2007) Biosci. Biotechnol. Biochem. , vol.71 , pp. 855-865
    • Horie, M.1    Fukui, K.2    Xie, M.3    Kageyama, Y.4    Hamada, K.5    Sakihama, Y.6    Sugimori, K.7    Matsumoto, K.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.