DOI: 10.1016/j.celrep.2014.09.011. Molecular Basis for the Ribosome Functioning as an L-Tryptophan Sensor

Molecular Basis for the Ribosome Functioning as an L-Tryptophan Sensor

10.1016/j.celrep.2014.09.011

Crossref journal-article

Elsevier BV

Cell Reports (78)

Bibliography

Bischoff, L., Berninghausen, O., & Beckmann, R. (2014). Molecular Basis for the Ribosome Functioning as an L-Tryptophan Sensor. Cell Reports, 9(2), 469â475.

Authors 3

Lukas Bischoff (first)
Otto Berninghausen (additional)
Roland Beckmann (additional)

References 29 Referenced 75

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10.1016/j.jsb.2006.06.001 / J. Struct. Biol. / SIGNATURE: a single-particle selection system for molecular electron microscopy by Chen (2007)
10.1128/JB.00290-08 / J. Bacteriol. / Conserved residues Asp16 and Pro24 of TnaC-tRNAPro participate in tryptophan induction of Tna operon expression by Cruz-Vera (2008)
10.1016/j.molcel.2005.06.013 / Mol. Cell / Features of ribosome-peptidyl-tRNA interactions essential for tryptophan induction of tna operon expression by Cruz-Vera (2005)
10.1073/pnas.0600082103 / Proc. Natl. Acad. Sci. USA / Changes produced by bound tryptophan in the ribosome peptidyl transferase center in response to TnaC, a nascent leader peptide by Cruz-Vera (2006)
10.1128/JB.01869-06 / J. Bacteriol. / Ribosomal features essential for tna operon induction: tryptophan binding at the peptidyl transferase center by Cruz-Vera (2007)
10.1128/JB.01002-09 / J. Bacteriol. / Tryptophan inhibits Proteus vulgaris TnaC leader peptide elongation, activating tna operon expression by Cruz-Vera (2009)
10.1073/pnas.1007988107 / Proc. Natl. Acad. Sci. USA / Structures of the Escherichia coli ribosome with antibiotics bound near the peptidyl transferase center explain spectra of drug action by Dunkle (2010)
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10.1006/jsbi.1996.0030 / J. Struct. Biol. / SPIDER and WEB: processing and visualization of images in 3D electron microscopy and related fields by Frank (1996)
10.1128/jb.177.24.7245-7254.1995 / J. Bacteriol. / Evidence suggesting cis action by the TnaC leader peptide in regulating transcription attenuation in the tryptophanase operon of Escherichia coli by Gish (1995)
10.1074/jbc.M008892200 / J. Biol. Chem. / Reproducing tna operon regulation in vitro in an S-30 system. Tryptophan induction inhibits cleavage of TnaC peptidyl-tRNA by Gong (2001)
10.1126/science.1073997 / Science / Instruction of translating ribosome by nascent peptide by Gong (2002)
10.1073/pnas.171299298 / Proc. Natl. Acad. Sci. USA / The mechanism of tryptophan induction of tryptophanase operon expression: tryptophan inhibits release factor-mediated cleavage of TnaC-peptidyl-tRNA(Pro) by Gong (2001)
10.1016/S0022-2836(03)00668-5 / J. Mol. Biol. / Structures of five antibiotics bound at the peptidyl transferase center of the large ribosomal subunit by Hansen (2003)
10.1146/annurev-biochem-080211-105026 / Annu. Rev. Biochem. / Arrest peptides: cis-acting modulators of translation by Ito (2013)
10.1073/pnas.1003995107 / Proc. Natl. Acad. Sci. USA / Structure of the 70S ribosome bound to release factor 2 and a substrate analog provides insights into catalysis of peptide release by Jin (2010)
10.1038/nmeth.2727 / Nat. Methods / Quantifying the local resolution of cryo-EM density maps by Kucukelbir (2014)
10.1093/nar/gkt923 / Nucleic Acids Res. / Interactions of the TnaC nascent peptide with rRNA in the exit tunnel enable the ribosome to respond to free tryptophan by Martínez (2014)
10.1073/pnas.0809211106 / Proc. Natl. Acad. Sci. USA / Slow peptide bond formation by proline and other N-alkylamino acids in translation by Pavlov (2009)
10.1002/jcc.20084 / J. Comput. Chem. / UCSF Chimera—a visualization system for exploratory research and analysis by Pettersen (2004)
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{'key': '10.1016/j.celrep.2014.09.011_bib24', 'first-page': '225', 'article-title': 'A pre-translocational intermediate in protein synthesis observed in crystals of enzymatically active 50S subunits', 'volume': '9', 'author': 'Schmeing', 'year': '2002', 'journal-title': 'Nat. Struct. Biol.'} / Nat. Struct. Biol. / A pre-translocational intermediate in protein synthesis observed in crystals of enzymatically active 50S subunits by Schmeing (2002)
10.1016/j.molcel.2005.09.006 / Mol. Cell / Structural insights into the roles of water and the 2′ hydroxyl of the P site tRNA in the peptidyl transferase reaction by Schmeing (2005)
10.1038/nature04152 / Nature / An induced-fit mechanism to promote peptide bond formation and exclude hydrolysis of peptidyl-tRNA by Schmeing (2005)
10.1126/science.1179700 / Science / The crystal structure of the ribosome bound to EF-Tu and aminoacyl-tRNA by Schmeing (2009)
10.1126/science.1177662 / Science / Structural insight into nascent polypeptide chain-mediated translational stalling by Seidelt (2009)
10.1016/j.str.2010.02.011 / Structure / Recognition of the regulatory nascent chain TnaC by the ribosome by Trabuco (2010)

Dates

Type	When
Created	10 years, 10 months ago (Oct. 9, 2014, 3:11 p.m.)
Deposited	6 years, 11 months ago (Sept. 28, 2018, 9:51 a.m.)
Indexed	2 months, 3 weeks ago (June 9, 2025, 10:26 a.m.)
Issued	10 years, 11 months ago (Oct. 1, 2014)
Published	10 years, 11 months ago (Oct. 1, 2014)
Published Print	10 years, 11 months ago (Oct. 1, 2014)

Funders 0

None

BibTeX

@article{Bischoff_2014, title={Molecular Basis for the Ribosome Functioning as an L-Tryptophan Sensor}, volume={9}, ISSN={2211-1247}, url={http://dx.doi.org/10.1016/j.celrep.2014.09.011}, DOI={10.1016/j.celrep.2014.09.011}, number={2}, journal={Cell Reports}, publisher={Elsevier BV}, author={Bischoff, Lukas and Berninghausen, Otto and Beckmann, Roland}, year={2014}, month=oct, pages={469–475} }

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      "label": "Content Type"
    },
    {
      "value": "Copyright \u00a9 2014 The Authors. Published by Elsevier Inc.",
      "name": "copyright",
      "label": "Copyright"
    }
  ]
}