메뉴 건너뛰기




Volumn 534, Issue 7606, 2016, Pages 277-280

Ribosome-dependent activation of stringent control

Author keywords

[No Author keywords available]

Indexed keywords

ANTIBIOTIC AGENT; TRANSFER RNA; ADENOSINE; AMINO ACID; AMINOACYL TRANSFER RNA; ESCHERICHIA COLI PROTEIN; GUANOSINE 3' DIPHOSPHATE 5' DIPHOSPHATE; GUANOSINE TRIPHOSPHATE PYROPHOSPHOKINASE;

EID: 84969814858     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature17675     Document Type: Article
Times cited : (167)

References (51)
  • 1
    • 0001763907 scopus 로고
    • The effects of a tryptophan-histidine deficiency in a mutant of Escherichia coli
    • Sands, M. K. & Roberts, R. B. The effects of a tryptophan-histidine deficiency in a mutant of Escherichia coli. J. Bacteriol. 63, 505-511 (1952).
    • (1952) J. Bacteriol. , vol.63 , pp. 505-511
    • Sands, M.K.1    Roberts, R.B.2
  • 2
    • 0000975897 scopus 로고
    • A genetic locus for the regulation of ribonucleic acid synthesis
    • Stent, G. S. & Brenner, S. A genetic locus for the regulation of ribonucleic acid synthesis. Proc. Natl Acad. Sci. USA 47, 2005-2014 (1961).
    • (1961) Proc. Natl Acad. Sci. USA , vol.47 , pp. 2005-2014
    • Stent, G.S.1    Brenner, S.2
  • 5
    • 2642638981 scopus 로고
    • Protein and ribonucleic acid synthesis in a mutant of Escherichia coli with an altered aminoacyl ribonucleic acid synthetase
    • Fangman, W. L. & Neidhardt, F. C. Protein and ribonucleic acid synthesis in a mutant of Escherichia coli with an altered aminoacyl ribonucleic acid synthetase. J. Biol. Chem. 239, 1844-1847 (1964).
    • (1964) J. Biol. Chem. , vol.239 , pp. 1844-1847
    • Fangman, W.L.1    Neidhardt, F.C.2
  • 6
    • 0007825206 scopus 로고
    • Synthesis of guanosine tetra- and pentaphosphate requires the presence of a codon-specific, uncharged transfer ribonucleic acid in the acceptor site of ribosomes
    • Haseltine, W. A. & Block, R. Synthesis of guanosine tetra- and pentaphosphate requires the presence of a codon-specific, uncharged transfer ribonucleic acid in the acceptor site of ribosomes. Proc. Natl Acad. Sci. USA 70, 1564-1568 (1973).
    • (1973) Proc. Natl Acad. Sci. USA , vol.70 , pp. 1564-1568
    • Haseltine, W.A.1    Block, R.2
  • 7
    • 0015817462 scopus 로고
    • Codon specific, tRNA dependent in vitro synthesis of ppGpp and pppGpp
    • Pedersen, F. S., Lund, E. & Kjeldgaard, N. O. Codon specific, tRNA dependent in vitro synthesis of ppGpp and pppGpp. Nat. New Biol. 243, 13-15 (1973).
    • (1973) Nat. New Biol. , vol.243 , pp. 13-15
    • Pedersen, F.S.1    Lund, E.2    Kjeldgaard, N.O.3
  • 8
    • 0015515019 scopus 로고
    • MSI and MSII made on ribosome in idling step of protein synthesis
    • Haseltine, W. A., Block, R., Gilbert, W. & Weber, K. MSI and MSII made on ribosome in idling step of protein synthesis. Nature 238, 381-384 (1972).
    • (1972) Nature , vol.238 , pp. 381-384
    • Haseltine, W.A.1    Block, R.2    Gilbert, W.3    Weber, K.4
  • 9
    • 0014478832 scopus 로고
    • Two compounds implicated in the function of the RC gene of Escherichia coli
    • Cashel, M. & Gallant, J. Two compounds implicated in the function of the RC gene of Escherichia coli. Nature 221, 838-841 (1969).
    • (1969) Nature , vol.221 , pp. 838-841
    • Cashel, M.1    Gallant, J.2
  • 10
    • 0014939550 scopus 로고
    • The control of ribonucleic acid synthesis in Escherichia coli. V. Characterization of a nucleotide associated with the stringent response
    • Cashel, M. & Kalbacher, B. The control of ribonucleic acid synthesis in Escherichia coli. V. Characterization of a nucleotide associated with the stringent response. J. Biol. Chem. 245, 2309-2318 (1970).
    • (1970) J. Biol. Chem. , vol.245 , pp. 2309-2318
    • Cashel, M.1    Kalbacher, B.2
  • 11
    • 79961217635 scopus 로고    scopus 로고
    • The RelA/SpoT homolog (RSH) superfamily: Distribution and functional evolution of ppGpp synthetases and hydrolases across the tree of life
    • Atkinson, G. C., Tenson, T. & Hauryliuk, V. The RelA/SpoT homolog (RSH) superfamily: distribution and functional evolution of ppGpp synthetases and hydrolases across the tree of life. PLoS One 6, e23479 (2011).
    • (2011) PLoS One , vol.6 , pp. e23479
    • Atkinson, G.C.1    Tenson, T.2    Hauryliuk, V.3
  • 12
    • 84955307962 scopus 로고    scopus 로고
    • Sampling the conformational space of the catalytic subunit of human γ-secretase
    • Bai, X.-C., Rajendra, E., Yang, G., Shi, Y. & Scheres, S. H. Sampling the conformational space of the catalytic subunit of human γ-secretase. elife 4, e11182 (2015).
    • (2015) Elife , vol.4 , pp. e11182
    • Bai, X.-C.1    Rajendra, E.2    Yang, G.3    Shi, Y.4    Scheres, S.H.5
  • 13
    • 84883487098 scopus 로고    scopus 로고
    • The ribosome triggers the stringent response by RelA via a highly distorted tRNA
    • Agirrezabala, X. et al. The ribosome triggers the stringent response by RelA via a highly distorted tRNA. EMBO Rep. 14, 811-816 (2013).
    • (2013) EMBO Rep. , vol.14 , pp. 811-816
    • Agirrezabala, X.1
  • 14
    • 70350588648 scopus 로고    scopus 로고
    • The crystal structure of the ribosome bound to EF-Tu and aminoacyl-tRNA
    • Schmeing, T. M. et al. The crystal structure of the ribosome bound to EF-Tu and aminoacyl-tRNA. Science 326, 688-694 (2009).
    • (2009) Science , vol.326 , pp. 688-694
    • Schmeing, T.M.1
  • 15
    • 33749354360 scopus 로고    scopus 로고
    • Structure of the 70S ribosome complexed with mRNA and tRNA
    • Selmer, M. Structure of the 70S ribosome complexed with mRNA and tRNA. Science 313, 1935-1942 (2006).
    • (2006) Science , vol.313 , pp. 1935-1942
    • Selmer, M.1
  • 16
    • 0022494313 scopus 로고
    • Affinities of tRNA binding sites of ribosomes from Escherichia coli
    • Lill, R., Robertson, J. M. & Wintermeyer, W. Affinities of tRNA binding sites of ribosomes from Escherichia coli. Biochemistry 25, 3245-3255 (1986).
    • (1986) Biochemistry , vol.25 , pp. 3245-3255
    • Lill, R.1    Robertson, J.M.2    Wintermeyer, W.3
  • 18
    • 0017040661 scopus 로고
    • Free 3′-OH group of the terminal adenosine of the tRNA molecule is essential for the synthesis in vitro of guanosine tetraphosphate and pentaphosphate in a ribosomal system from Escherichia coli
    • Sprinzl, M. & Richter, D. Free 3′-OH group of the terminal adenosine of the tRNA molecule is essential for the synthesis in vitro of guanosine tetraphosphate and pentaphosphate in a ribosomal system from Escherichia coli. Eur. J. Biochem. 71, 171-176 (1976).
    • (1976) Eur. J. Biochem. , vol.71 , pp. 171-176
    • Sprinzl, M.1    Richter, D.2
  • 19
    • 0016299779 scopus 로고
    • A new relaxed mutant of Escherichia coli with an altered 50S ribosomal subunit
    • Friesen, J. D., Fiil, N. P., Parker, J. M. & Haseltine, W. A. A new relaxed mutant of Escherichia coli with an altered 50S ribosomal subunit. Proc. Natl Acad. Sci. USA 71, 3465-3469 (1974).
    • (1974) Proc. Natl Acad. Sci. USA , vol.71 , pp. 3465-3469
    • Friesen, J.D.1    Fiil, N.P.2    Parker, J.M.3    Haseltine, W.A.4
  • 21
    • 0035150018 scopus 로고    scopus 로고
    • Regulation of Escherichia coli RelA requires oligomerization of the C-terminal domain
    • Gropp, M., Strausz, Y., Gross, M. & Glaser, G. Regulation of Escherichia coli RelA requires oligomerization of the C-terminal domain. J. Bacteriol. 183, 570-579 (2001).
    • (2001) J. Bacteriol. , vol.183 , pp. 570-579
    • Gropp, M.1    Strausz, Y.2    Gross, M.3    Glaser, G.4
  • 22
    • 0025857678 scopus 로고
    • Overexpression of the relA gene in Escherichia coli
    • Schreiber, G. et al. Overexpression of the relA gene in Escherichia coli. J. Biol. Chem. 266, 3760-3767 (1991).
    • (1991) J. Biol. Chem. , vol.266 , pp. 3760-3767
    • Schreiber, G.1
  • 23
    • 0037963475 scopus 로고    scopus 로고
    • Locking and unlocking of ribosomal motions
    • Valle, M. et al. Locking and unlocking of ribosomal motions. Cell 114, 123-134 (2003).
    • (2003) Cell , vol.114 , pp. 123-134
    • Valle, M.1
  • 24
    • 18544377013 scopus 로고    scopus 로고
    • The RNA recognition motif, a plastic RNA-binding platform to regulate post-transcriptional gene expression
    • Maris, C., Dominguez, C. & Allain, F. H. T. The RNA recognition motif, a plastic RNA-binding platform to regulate post-transcriptional gene expression. FEBS J. 272, 2118-2131 (2005).
    • (2005) FEBS J. , vol.272 , pp. 2118-2131
    • Maris, C.1    Dominguez, C.2    Allain, F.H.T.3
  • 25
    • 1842766260 scopus 로고    scopus 로고
    • Conformational antagonism between opposing active sites in a bifunctional RelA/SpoT homolog modulates (p)ppGpp metabolism during the stringent response
    • Hogg, T., Mechold, U., Malke, H., Cashel, M. & Hilgenfeld, R. Conformational antagonism between opposing active sites in a bifunctional RelA/SpoT homolog modulates (p)ppGpp metabolism during the stringent response. Cell 117, 57-68 (2004).
    • (2004) Cell , vol.117 , pp. 57-68
    • Hogg, T.1    Mechold, U.2    Malke, H.3    Cashel, M.4    Hilgenfeld, R.5
  • 26
    • 0035688236 scopus 로고    scopus 로고
    • Dimerization of the RelA protein of Escherichia coli
    • Yang, X. & Ishiguro, E. E. Dimerization of the RelA protein of Escherichia coli. Biochem. Cell Biol. 79, 729-736 (2001).
    • (2001) Biochem. Cell Biol. , vol.79 , pp. 729-736
    • Yang, X.1    Ishiguro, E.E.2
  • 27
    • 79961224232 scopus 로고    scopus 로고
    • Single-molecule investigations of the stringent response machinery in living bacterial cells
    • English, B. P. et al. Single-molecule investigations of the stringent response machinery in living bacterial cells. Proc. Natl Acad. Sci. USA 108, E365-E373 (2011).
    • (2011) Proc. Natl Acad. Sci. USA , vol.108 , pp. E365-E373
    • English, B.P.1
  • 28
    • 84878924244 scopus 로고    scopus 로고
    • Structural basis of the translational elongation cycle
    • Voorhees, R. M. & Ramakrishnan, V. Structural basis of the translational elongation cycle. Annu. Rev. Biochem. 82, 203-236 (2013).
    • (2013) Annu. Rev. Biochem. , vol.82 , pp. 203-236
    • Voorhees, R.M.1    Ramakrishnan, V.2
  • 29
    • 84956587413 scopus 로고    scopus 로고
    • Effects of amino acid starvation on RelA diffusive behavior in live Escherichia coli
    • Li, W. et al. Effects of amino acid starvation on RelA diffusive behavior in live Escherichia coli. Mol. Microbiol. 99, 571-585 (2016).
    • (2016) Mol. Microbiol. , vol.99 , pp. 571-585
    • Li, W.1
  • 30
    • 81555212273 scopus 로고    scopus 로고
    • Active starvation responses mediate antibiotic tolerance in biofilms and nutrient-limited bacteria
    • Nguyen, D. et al. Active starvation responses mediate antibiotic tolerance in biofilms and nutrient-limited bacteria. Science 334, 982-986 (2011).
    • (2011) Science , vol.334 , pp. 982-986
    • Nguyen, D.1
  • 31
    • 84880848354 scopus 로고    scopus 로고
    • Electron counting and beam-induced motion correction enable near-atomic-resolution single-particle cryo-EM
    • Li, X. et al. Electron counting and beam-induced motion correction enable near-atomic-resolution single-particle cryo-EM. Nat. Methods 10, 584-590 (2013).
    • (2013) Nat. Methods , vol.10 , pp. 584-590
    • Li, X.1
  • 32
    • 84955216953 scopus 로고    scopus 로고
    • Gctf: Real-time CTF determination and correction
    • Zhang, K. Gctf: real-time CTF determination and correction. J. Struct. Biol. 193, 1-12 (2015).
    • (2015) J. Struct. Biol. , vol.193 , pp. 1-12
    • Zhang, K.1
  • 33
    • 33845332754 scopus 로고    scopus 로고
    • EMAN2: An extensible image processing suite for electron microscopy
    • Tang, G. et al. EMAN2: an extensible image processing suite for electron microscopy. J. Struct. Biol. 157, 38-46 (2007).
    • (2007) J. Struct. Biol. , vol.157 , pp. 38-46
    • Tang, G.1
  • 34
    • 84868444740 scopus 로고    scopus 로고
    • RELION: Implementation of a Bayesian approach to cryo-EM structure determination
    • Scheres, S. H. W. RELION: implementation of a Bayesian approach to cryo-EM structure determination. J. Struct. Biol. 180, 519-530 (2012).
    • (2012) J. Struct. Biol. , vol.180 , pp. 519-530
    • Scheres, S.H.W.1
  • 35
    • 84920942671 scopus 로고    scopus 로고
    • Beam-induced motion correction for sub-megadalton cryo-EM particles
    • Scheres, S. H. Beam-induced motion correction for sub-megadalton cryo-EM particles. elife 3, e03665 (2014).
    • (2014) Elife , vol.3 , pp. e03665
    • Scheres, S.H.1
  • 36
    • 0142042865 scopus 로고    scopus 로고
    • Optimal determination of particle orientation, absolute hand, and contrast loss in single-particle electron cryomicroscopy
    • Rosenthal, P. B. & Henderson, R. Optimal determination of particle orientation, absolute hand, and contrast loss in single-particle electron cryomicroscopy. J. Mol. Biol. 333, 721-745 (2003).
    • (2003) J. Mol. Biol. , vol.333 , pp. 721-745
    • Rosenthal, P.B.1    Henderson, R.2
  • 37
    • 84894623755 scopus 로고    scopus 로고
    • Quantifying the local resolution of cryo-EM density maps
    • Kucukelbir, A., Sigworth, F. J. & Tagare, H. D. Quantifying the local resolution of cryo-EM density maps. Nat. Methods 11, 63-65 (2013).
    • (2013) Nat. Methods , vol.11 , pp. 63-65
    • Kucukelbir, A.1    Sigworth, F.J.2    Tagare, H.D.3
  • 38
    • 84926406635 scopus 로고    scopus 로고
    • High-resolution structure of the Escherichia coli ribosome
    • Noeske, J. et al. High-resolution structure of the Escherichia coli ribosome. Nat. Struct. Mol. Biol. 22, 336-341 (2015).
    • (2015) Nat. Struct. Mol. Biol. , vol.22 , pp. 336-341
    • Noeske, J.1
  • 39
    • 4444221565 scopus 로고    scopus 로고
    • UCSF Chimera-A visualization system for exploratory research and analysis
    • Pettersen, E. F. et al. UCSF Chimera-a visualization system for exploratory research and analysis. J. Comput. Chem. 25, 1605-1612 (2004).
    • (2004) J. Comput. Chem. , vol.25 , pp. 1605-1612
    • Pettersen, E.F.1
  • 40
    • 84928560614 scopus 로고    scopus 로고
    • Structure of the E. Coli ribosome-EF-Tu complex at <3 Å resolution by Cs-corrected cryo-EM
    • Fischer, N. et al. Structure of the E. coli ribosome-EF-Tu complex at <3 Å resolution by Cs-corrected cryo-EM. Nature 520, 567-570 (2015).
    • (2015) Nature , vol.520 , pp. 567-570
    • Fischer, N.1
  • 41
    • 78149302861 scopus 로고    scopus 로고
    • The mechanism for activation of GTP hydrolysis on the ribosome
    • Voorhees, R. M., Schmeing, T. M., Kelley, A. C. & Ramakrishnan, V. The mechanism for activation of GTP hydrolysis on the ribosome. Science 330, 835-838 (2010).
    • (2010) Science , vol.330 , pp. 835-838
    • Voorhees, R.M.1    Schmeing, T.M.2    Kelley, A.C.3    Ramakrishnan, V.4
  • 42
    • 34547696927 scopus 로고    scopus 로고
    • Structural basis for aminoglycoside inhibition of bacterial ribosome recycling
    • Borovinskaya, M. A. et al. Structural basis for aminoglycoside inhibition of bacterial ribosome recycling. Nat. Struct. Mol. Biol. 14, 727-732 (2007).
    • (2007) Nat. Struct. Mol. Biol. , vol.14 , pp. 727-732
    • Borovinskaya, M.A.1
  • 43
    • 39449115394 scopus 로고    scopus 로고
    • I-TASSER server for protein 3D structure prediction
    • Zhang, Y. I-TASSER server for protein 3D structure prediction. BMC Bioinformatics 9, 40 (2008).
    • (2008) BMC Bioinformatics , vol.9 , pp. 40
    • Zhang, Y.1
  • 44
    • 84921777915 scopus 로고    scopus 로고
    • Tools for macromolecular model building and refinement into electron cryo-microscopy reconstructions
    • Brown, A. et al. Tools for macromolecular model building and refinement into electron cryo-microscopy reconstructions. Acta Crystallogr. D 71, 136-153 (2015).
    • (2015) Acta Crystallogr. D , vol.71 , pp. 136-153
    • Brown, A.1
  • 45
    • 74549178560 scopus 로고    scopus 로고
    • MolProbity: All-atom structure validation for macromolecular crystallography
    • Chen, V. B. et al. MolProbity: all-atom structure validation for macromolecular crystallography. Acta Crystallogr. D 66, 12-21 (2009).
    • (2009) Acta Crystallogr. D , vol.66 , pp. 12-21
    • Chen, V.B.1
  • 46
    • 84897000112 scopus 로고    scopus 로고
    • Structure of the yeast mitochondrial large ribosomal subunit
    • Amunts, A. et al. Structure of the yeast mitochondrial large ribosomal subunit. Science 343, 1485-1489 (2014).
    • (2014) Science , vol.343 , pp. 1485-1489
    • Amunts, A.1
  • 49
    • 0030815133 scopus 로고    scopus 로고
    • Raster3D: Photorealistic molecular graphics
    • Merritt, E. A. & Bacon, D. J. Raster3D: photorealistic molecular graphics. Methods Enzymol. 277, 505-524 (1997).
    • (1997) Methods Enzymol. , vol.277 , pp. 505-524
    • Merritt, E.A.1    Bacon, D.J.2
  • 50
    • 82255194257 scopus 로고    scopus 로고
    • Automatic generation of protein structure cartoons with Pro-origami
    • Stivala, A., Wybrow, M., Wirth, A., Whisstock, J. C. & Stuckey, P. J. Automatic generation of protein structure cartoons with Pro-origami. Bioinformatics 27, 3315-3316 (2011).
    • (2011) Bioinformatics , vol.27 , pp. 3315-3316
    • Stivala, A.1    Wybrow, M.2    Wirth, A.3    Whisstock, J.C.4    Stuckey, P.J.5
  • 51
    • 0035964342 scopus 로고    scopus 로고
    • Electrostatics of nanosystems: Application to microtubules and the ribosome
    • Baker, N. A., Sept, D., Joseph, S. & Holst, M. J. Electrostatics of nanosystems: application to microtubules and the ribosome. Proc. Natl Acad. Sci. USA 98, 10037-10041 (2001).
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 10037-10041
    • Baker, N.A.1    Sept, D.2    Joseph, S.3    Holst, M.J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.