메뉴 건너뛰기




Volumn 15, Issue 2, 2009, Pages 208-214

A signal relay between ribosomal protein S12 and elongation factor EF-Tu during decoding of mRNA

Author keywords

Decoding; EF Tu; Ribosomal protein S12; Ribosome; Streptomycin

Indexed keywords

ELONGATION FACTOR TU; GUANOSINE TRIPHOSPHATASE; MESSENGER RNA; MOCIMYCIN; RNA 12S; RNA 16S; STREPTOMYCIN; TRANSFER RNA;

EID: 58249120107     PISSN: 13558382     EISSN: 14699001     Source Type: Journal    
DOI: 10.1261/rna.1355709     Document Type: Article
Times cited : (24)

References (29)
  • 2
    • 0026521547 scopus 로고
    • Kinetic properties of Escherichia coli ribosomes with altered forms of S12
    • Bilgin, N., Claesens, F., Pahverk, H., and Ehrenberg, M. 1992. Kinetic properties of Escherichia coli ribosomes with altered forms of S12. J. Mol. Biol. 224: 1011-1027.
    • (1992) J. Mol. Biol , vol.224 , pp. 1011-1027
    • Bilgin, N.1    Claesens, F.2    Pahverk, H.3    Ehrenberg, M.4
  • 3
    • 18244364594 scopus 로고    scopus 로고
    • Severity of the streptomycin resistance and streptomycin dependence phenotypes of ribosomal protein S12 of Thermus thermophilus depends on the identity of highly conserved amino acid residues
    • Carr, J.F., Gregory, S.T., and Dahlberg, A.E. 2005. Severity of the streptomycin resistance and streptomycin dependence phenotypes of ribosomal protein S12 of Thermus thermophilus depends on the identity of highly conserved amino acid residues. J. Bacteriol. 18: 3548-3550.
    • (2005) J. Bacteriol , vol.18 , pp. 3548-3550
    • Carr, J.F.1    Gregory, S.T.2    Dahlberg, A.E.3
  • 4
    • 0347059426 scopus 로고    scopus 로고
    • Structural studies of the 30S ribosomal subunit
    • Ph.D. thesis, University of Cambridge, Cambridge, UK
    • Carter, A.P. 2002. "Structural studies of the 30S ribosomal subunit." Ph.D. thesis, University of Cambridge, Cambridge, UK.
    • (2002)
    • Carter, A.P.1
  • 5
    • 0034699519 scopus 로고    scopus 로고
    • Functional insights from the structure of the 30S ribosomal subunit and its interactions with antibiotics
    • Carter, A.P., Clemons, W.M., Brodersen, D.E., Morgan-Warren, R.J., Wimberly, B.T., and Ramakrishnan, V. 2000. Functional insights from the structure of the 30S ribosomal subunit and its interactions with antibiotics. Nature 407: 340-348.
    • (2000) Nature , vol.407 , pp. 340-348
    • Carter, A.P.1    Clemons, W.M.2    Brodersen, D.E.3    Morgan-Warren, R.J.4    Wimberly, B.T.5    Ramakrishnan, V.6
  • 6
    • 18844408328 scopus 로고    scopus 로고
    • An active role for tRNA in decoding beyond codon:anticodon pairing
    • Cochella, L. and Green, R. 2005. An active role for tRNA in decoding beyond codon:anticodon pairing. Science 308: 1178-1180.
    • (2005) Science , vol.308 , pp. 1178-1180
    • Cochella, L.1    Green, R.2
  • 8
    • 0019851108 scopus 로고
    • A kirromycin resistant elongation factor EF-Tu from Escherichia coli contains a threonine instead of an alanine in position 375
    • Duisterwinkel, F.J., de Graaf, J.M., Kraal, B., and Bosch, L. 1981. A kirromycin resistant elongation factor EF-Tu from Escherichia coli contains a threonine instead of an alanine in position 375. FEBS Lett. 131: 89-93.
    • (1981) FEBS Lett , vol.131 , pp. 89-93
    • Duisterwinkel, F.J.1    de Graaf, J.M.2    Kraal, B.3    Bosch, L.4
  • 9
    • 0035367324 scopus 로고    scopus 로고
    • Streptomycin-resistant and streptomycin-dependent mutants of the extreme thermophile Thermus thermophilus
    • Gregory, S.T., Cate, J.H.D., and Dahlberg, A.E. 2001. Streptomycin-resistant and streptomycin-dependent mutants of the extreme thermophile Thermus thermophilus. J. Mol. Biol. 309: 333-338.
    • (2001) J. Mol. Biol , vol.309 , pp. 333-338
    • Gregory, S.T.1    Cate, J.H.D.2    Dahlberg, A.E.3
  • 10
    • 21844446585 scopus 로고    scopus 로고
    • Mutational analysis of 16S and 23S rRNA genes of Thermus thermophilus
    • Gregory, S.T., Carr, J.F., Rodriguez-Correa, D., and Dahlberg, A.E. 2005. Mutational analysis of 16S and 23S rRNA genes of Thermus thermophilus. J. Bacteriol. 187: 4804-4812.
    • (2005) J. Bacteriol , vol.187 , pp. 4804-4812
    • Gregory, S.T.1    Carr, J.F.2    Rodriguez-Correa, D.3    Dahlberg, A.E.4
  • 11
    • 1842420639 scopus 로고    scopus 로고
    • Streptomycin interferes with conformational coupling between codon recognition and GTPase activation on the ribosome
    • Gromadski, K.B. and Rodnina, M.V. 2004. Streptomycin interferes with conformational coupling between codon recognition and GTPase activation on the ribosome. Nat. Struct. Mol. Biol. 11: 316-322.
    • (2004) Nat. Struct. Mol. Biol , vol.11 , pp. 316-322
    • Gromadski, K.B.1    Rodnina, M.V.2
  • 12
    • 0015223081 scopus 로고
    • Tryptophan transfer RNA as the UGA suppressor
    • Hirsh, D. 1971. Tryptophan transfer RNA as the UGA suppressor. J. Mol. Biol. 58: 439-458.
    • (1971) J. Mol. Biol , vol.58 , pp. 439-458
    • Hirsh, D.1
  • 13
    • 0022448655 scopus 로고
    • Genetic transformation of the extreme thermophile Thermus thermophilus and of other Thermus spp
    • Koyama, Y., Hoshino, T., Tomizuka, N., and Furukawa, K. 1986. Genetic transformation of the extreme thermophile Thermus thermophilus and of other Thermus spp. J. Bacteriol. 166: 338-340.
    • (1986) J. Bacteriol , vol.166 , pp. 338-340
    • Koyama, Y.1    Hoshino, T.2    Tomizuka, N.3    Furukawa, K.4
  • 14
    • 0023019537 scopus 로고
    • Isolation of halotolerant Thermus spp. from submarine hot springs in Iceland
    • Kristjansson, J.K., Hreggvidsson, G.O., and Alfredsson, G.A. 1986. Isolation of halotolerant Thermus spp. from submarine hot springs in Iceland. Appl. Environ. Microbiol. 52: 1313-1316.
    • (1986) Appl. Environ. Microbiol , vol.52 , pp. 1313-1316
    • Kristjansson, J.K.1    Hreggvidsson, G.O.2    Alfredsson, G.A.3
  • 15
    • 0000190405 scopus 로고    scopus 로고
    • Limitations of translational accuracy
    • eds. F.C. Neidhardt et al, pp, American Society for Microbiology, Washington, DC
    • Kurland, C.G., Hughes, D., and Ehrenberg, M. 1996. Limitations of translational accuracy. In Escherichia coli and Salmonella: Cellular and molecular biology (eds. F.C. Neidhardt et al.), pp. 979-1004. American Society for Microbiology, Washington, DC.
    • (1996) Escherichia coli and Salmonella: Cellular and molecular biology , pp. 979-1004
    • Kurland, C.G.1    Hughes, D.2    Ehrenberg, M.3
  • 16
    • 18844413446 scopus 로고    scopus 로고
    • Structural insights into translational fidelity
    • Ogle, J.M. and Ramakrishnan, V. 2005. Structural insights into translational fidelity. Annu. Rev. Biochem. 74: 129-177.
    • (2005) Annu. Rev. Biochem , vol.74 , pp. 129-177
    • Ogle, J.M.1    Ramakrishnan, V.2
  • 18
    • 0037184536 scopus 로고    scopus 로고
    • Ogle, J.M., Murphy IV., F.V., Tarry, M.J., and Ramakrishnan, V. 2002. Selection of tRNA by the ribosome requires a transition from an open to a closed form. Cell 111: 721-732.
    • Ogle, J.M., Murphy IV., F.V., Tarry, M.J., and Ramakrishnan, V. 2002. Selection of tRNA by the ribosome requires a transition from an open to a closed form. Cell 111: 721-732.
  • 19
    • 0038403669 scopus 로고    scopus 로고
    • Insights into the decoding mechanism from recent ribosome structures
    • Ogle, J.M., Carter, A.P., and Ramakrishnan, V. 2003. Insights into the decoding mechanism from recent ribosome structures. Trends Biochem. Sci. 28: 259-266.
    • (2003) Trends Biochem. Sci , vol.28 , pp. 259-266
    • Ogle, J.M.1    Carter, A.P.2    Ramakrishnan, V.3
  • 20
    • 33746882485 scopus 로고    scopus 로고
    • Elongation factor Tu-targeted antibiotics: Four different structures, two mechanisms of action
    • Parmeggiani, A. and Nissen, P. 2006. Elongation factor Tu-targeted antibiotics: Four different structures, two mechanisms of action. FEBS Lett. 580: 4576-4581.
    • (2006) FEBS Lett , vol.580 , pp. 4576-4581
    • Parmeggiani, A.1    Nissen, P.2
  • 21
    • 0034700993 scopus 로고    scopus 로고
    • Intact aminoacyl-tRNA is required to trigger GTP hydrolysis by elongation factor Tu on the ribosome
    • Piepenburg, O., Pape, T., Pleiss, J.A., Wintermeyer, W., Uhlenbeck, O.C., and Rodnina, M.V. 2000. Intact aminoacyl-tRNA is required to trigger GTP hydrolysis by elongation factor Tu on the ribosome. Biochemistry 39: 1734-1738.
    • (2000) Biochemistry , vol.39 , pp. 1734-1738
    • Piepenburg, O.1    Pape, T.2    Pleiss, J.A.3    Wintermeyer, W.4    Uhlenbeck, O.C.5    Rodnina, M.V.6
  • 22
    • 14544285163 scopus 로고    scopus 로고
    • Recognition and selection of tRNA in translation
    • Rodnina, M.V., Gromadski, K.B., Kothe, U., and Wieden, H.J. 2005. Recognition and selection of tRNA in translation. FEBS Lett. 579: 938-942.
    • (2005) FEBS Lett , vol.579 , pp. 938-942
    • Rodnina, M.V.1    Gromadski, K.B.2    Kothe, U.3    Wieden, H.J.4
  • 23
    • 0021831282 scopus 로고
    • Mutant species of EF-Tu, altered at position 375, exhibit a reduced affinity for aminoacylated transfer-RNAs
    • Sam, T., Pingoud, A., and Bosch, L. 1985. Mutant species of EF-Tu, altered at position 375, exhibit a reduced affinity for aminoacylated transfer-RNAs. FEBS Lett. 185: 51-56.
    • (1985) FEBS Lett , vol.185 , pp. 51-56
    • Sam, T.1    Pingoud, A.2    Bosch, L.3
  • 24
    • 35748984942 scopus 로고    scopus 로고
    • Mutational analysis of S12 protein and implications for the accuracy of decoding by the ribosome
    • Sharma, D., Cukras, A.R., Rogers, E.J., Southworth, D.R., and Green, R. 2007. Mutational analysis of S12 protein and implications for the accuracy of decoding by the ribosome. J. Mol. Biol. 374: 1065-1076.
    • (2007) J. Mol. Biol , vol.374 , pp. 1065-1076
    • Sharma, D.1    Cukras, A.R.2    Rogers, E.J.3    Southworth, D.R.4    Green, R.5
  • 25
    • 0036829080 scopus 로고    scopus 로고
    • Ribosome interactions of aminoacyl-tRNA and elongation factor Tu in the codon-recognition complex
    • Stark, H., Rodnina, M.V., Wieden, H.J., Zemlin, F., Wintermeyer, W., and van Heel, M. 2002. Ribosome interactions of aminoacyl-tRNA and elongation factor Tu in the codon-recognition complex. Nat. Struct. Biol. 9: 849-854.
    • (2002) Nat. Struct. Biol , vol.9 , pp. 849-854
    • Stark, H.1    Rodnina, M.V.2    Wieden, H.J.3    Zemlin, F.4    Wintermeyer, W.5    van Heel, M.6
  • 26
    • 0027323589 scopus 로고
    • Double, independent mutational events in the rpsL gene of Escherichia coli: An example of hypermutability?
    • Timms, A.R. and Bridges, B.A. 1993. Double, independent mutational events in the rpsL gene of Escherichia coli: An example of hypermutability? Mol. Microbiol. 9: 335-342.
    • (1993) Mol. Microbiol , vol.9 , pp. 335-342
    • Timms, A.R.1    Bridges, B.A.2
  • 27
    • 0025866195 scopus 로고
    • Mutant ribosomes can generate dominant kirromycin resistance
    • Tubulekas, I., Buckingham, R.H., and Hughes, D. 1991. Mutant ribosomes can generate dominant kirromycin resistance. J. Bacteriol. 173: 3635-3643.
    • (1991) J. Bacteriol , vol.173 , pp. 3635-3643
    • Tubulekas, I.1    Buckingham, R.H.2    Hughes, D.3
  • 29
    • 0033990904 scopus 로고    scopus 로고
    • The effect of mutations in EF-Tu on its affinity for tRNA as measured by two novel and independent methods of general applicability
    • Vorstenbosch, E.L., Potapov, A.P., de Graaf, J.M., and Kraal, B. 2000. The effect of mutations in EF-Tu on its affinity for tRNA as measured by two novel and independent methods of general applicability. J. Biochem. Biophys. Methods 42: 1-14.
    • (2000) J. Biochem. Biophys. Methods , vol.42 , pp. 1-14
    • Vorstenbosch, E.L.1    Potapov, A.P.2    de Graaf, J.M.3    Kraal, B.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.