Open Access

Molecular Cell, volume 58, issue 5, pages 832-844

Distinct tRNA Accommodation Intermediates Observed on the Ribosome with the Antibiotics Hygromycin A and A201A

Polikanov Yury S ^{1, 2}

Starosta Agata L ³

Juette Manuel F ⁴

Altman Roger B ⁴

Terry Daniel S ⁴

Lu Wanli ⁵

Burnett Benjamin J ⁴

Dinos George P. ⁶

Reynolds Kevin R. ⁵

Blanchard Scott ⁷

Steitz Thomas A. ^{1, 8}

Wilson Daniel W. ^{3, 9}

Hide authors affiliations Show authors affiliations: 9 affiliations

Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520, USA |

Howard Hughes Medical Institute, Chevy Chase, MD 20815, USA. |

Gene Center and Department for Biochemistry, University of Munich, Feodor-Lynenstr. 25, 81377 Munich, Germany |

⁴

Department of Physiology and Biophysics, Weill Medical College of Cornell University, New York, NY 10065, USA. |

⁵

Department of Chemistry, Portland State University, Portland, OR 97207 USA |

⁶

Department of Biochemistry, School of Medicine, University of Patras, 26500, Patras, Greece |

⁷

Department of Physiology and Biophysics, Weill Medical College of Cornell University, New York, NY 10065, USA |

⁸

Howard Hughes Medical Institute, Chevy Chase, MD 20815, USA |

⁹

Center for integrated Protein Science Munich (CiPSM), University of Munich, Feodor-Lynenstr. 25, 81377 Munich, Germany |

Publication type: Journal Article

Publication date: 2015-06-01

Elsevier

Journal: Molecular Cell

Quartile SCImago

Quartile WOS

Impact factor: 16

ISSN: 10972765, 10974164

DOI: 10.1016/j.molcel.2015.04.014

Copy DOI

PubMed ID: 26028538

Molecular Biology

Cell Biology

Abstract

The increase in multi-drug-resistant bacteria is limiting the effectiveness of currently approved antibiotics, leading to a renewed interest in antibiotics with distinct chemical scaffolds. We have solved the structures of the Thermus thermophilus 70S ribosome with A-, P-, and E-site tRNAs bound and in complex with either the aminocyclitol-containing antibiotic hygromycin A (HygA) or the nucleoside antibiotic A201A. Both antibiotics bind at the peptidyl transferase center and sterically occlude the CCA-end of the A-tRNA from entering the A site of the peptidyl transferase center. Single-molecule Förster resonance energy transfer (smFRET) experiments reveal that HygA and A201A specifically interfere with full accommodation of the A-tRNA, leading to the presence of tRNA accommodation intermediates and thereby inhibiting peptide bond formation. Thus, our results provide not only insight into the mechanism of action of HygA and A201A, but also into the fundamental process of tRNA accommodation during protein synthesis.

By date By citations

Citations by journals

	1 2 3 4 5 6 7 8 9
Nucleic Acids Research	Nucleic Acids Research, 9, 11.54% Nucleic Acids Research 9 publications, 11.54%
Nature Communications	Nature Communications, 8, 10.26% Nature Communications 8 publications, 10.26%
Nature Chemical Biology	Nature Chemical Biology, 5, 6.41% Nature Chemical Biology 5 publications, 6.41%
Proceedings of the National Academy of Sciences of the United States of America	Proceedings of the National Academy of Sciences of the United States of America, 4, 5.13% Proceedings of the National Academy of Sciences of the United States of America 4 publications, 5.13%
International Journal of Molecular Sciences	International Journal of Molecular Sciences, 2, 2.56% International Journal of Molecular Sciences 2 publications, 2.56%
Nature	Nature, 2, 2.56% Nature 2 publications, 2.56%
Molecular Cell	Molecular Cell, 2, 2.56% Molecular Cell 2 publications, 2.56%
Angewandte Chemie	Angewandte Chemie, 2, 2.56% Angewandte Chemie 2 publications, 2.56%
Angewandte Chemie - International Edition	Angewandte Chemie - International Edition, 2, 2.56% Angewandte Chemie - International Edition 2 publications, 2.56%
Journal of the American Chemical Society	Journal of the American Chemical Society, 2, 2.56% Journal of the American Chemical Society 2 publications, 2.56%
Antimicrobial Agents and Chemotherapy	Antimicrobial Agents and Chemotherapy, 2, 2.56% Antimicrobial Agents and Chemotherapy 2 publications, 2.56%
Journal of Chemical Physics	Journal of Chemical Physics, 1, 1.28% Journal of Chemical Physics 1 publication, 1.28%
Philosophical Transactions of the Royal Society B: Biological Sciences	Philosophical Transactions of the Royal Society B: Biological Sciences, 1, 1.28% Philosophical Transactions of the Royal Society B: Biological Sciences 1 publication, 1.28%
Microorganisms	Microorganisms, 1, 1.28% Microorganisms 1 publication, 1.28%
Journal of Antibiotics	Journal of Antibiotics, 1, 1.28% Journal of Antibiotics 1 publication, 1.28%
World Journal of Microbiology and Biotechnology	World Journal of Microbiology and Biotechnology, 1, 1.28% World Journal of Microbiology and Biotechnology 1 publication, 1.28%
Nature Microbiology	Nature Microbiology, 1, 1.28% Nature Microbiology 1 publication, 1.28%
Biophysical Journal	Biophysical Journal, 1, 1.28% Biophysical Journal 1 publication, 1.28%
Biotechnology Advances	Biotechnology Advances, 1, 1.28% Biotechnology Advances 1 publication, 1.28%
Cell Host and Microbe	Cell Host and Microbe, 1, 1.28% Cell Host and Microbe 1 publication, 1.28%
Cell	Cell, 1, 1.28% Cell 1 publication, 1.28%
Research in Microbiology	Research in Microbiology, 1, 1.28% Research in Microbiology 1 publication, 1.28%
Microbiology spectrum	Microbiology spectrum, 1, 1.28% Microbiology spectrum 1 publication, 1.28%
BioEssays	BioEssays, 1, 1.28% BioEssays 1 publication, 1.28%
Medicinal Research Reviews	Medicinal Research Reviews, 1, 1.28% Medicinal Research Reviews 1 publication, 1.28%
Journal of Physical Chemistry B	Journal of Physical Chemistry B, 1, 1.28% Journal of Physical Chemistry B 1 publication, 1.28%
Journal of Medicinal Chemistry	Journal of Medicinal Chemistry, 1, 1.28% Journal of Medicinal Chemistry 1 publication, 1.28%
Organic and Biomolecular Chemistry	Organic and Biomolecular Chemistry, 1, 1.28% Organic and Biomolecular Chemistry 1 publication, 1.28%
Biochemistry (Moscow)	Biochemistry (Moscow), 1, 1.28% Biochemistry (Moscow) 1 publication, 1.28%
	1 2 3 4 5 6 7 8 9

Citations by publishers

	2 4 6 8 10 12 14 16 18
Springer Nature	Springer Nature, 18, 23.08% Springer Nature 18 publications, 23.08%
Oxford University Press	Oxford University Press, 9, 11.54% Oxford University Press 9 publications, 11.54%
Elsevier	Elsevier, 7, 8.97% Elsevier 7 publications, 8.97%
Wiley	Wiley, 6, 7.69% Wiley 6 publications, 7.69%
American Chemical Society (ACS)	American Chemical Society (ACS), 4, 5.13% American Chemical Society (ACS) 4 publications, 5.13%
Proceedings of the National Academy of Sciences (PNAS)	Proceedings of the National Academy of Sciences (PNAS), 4, 5.13% Proceedings of the National Academy of Sciences (PNAS) 4 publications, 5.13%
Multidisciplinary Digital Publishing Institute (MDPI)	Multidisciplinary Digital Publishing Institute (MDPI), 3, 3.85% Multidisciplinary Digital Publishing Institute (MDPI) 3 publications, 3.85%
American Society for Microbiology	American Society for Microbiology, 3, 3.85% American Society for Microbiology 3 publications, 3.85%
Annual Reviews	Annual Reviews, 2, 2.56% Annual Reviews 2 publications, 2.56%
American Institute of Physics (AIP)	American Institute of Physics (AIP), 1, 1.28% American Institute of Physics (AIP) 1 publication, 1.28%
The Royal Society	The Royal Society, 1, 1.28% The Royal Society 1 publication, 1.28%
Biophysical Society	Biophysical Society, 1, 1.28% Biophysical Society 1 publication, 1.28%
Royal Society of Chemistry (RSC)	Royal Society of Chemistry (RSC), 1, 1.28% Royal Society of Chemistry (RSC) 1 publication, 1.28%
Pleiades Publishing	Pleiades Publishing, 1, 1.28% Pleiades Publishing 1 publication, 1.28%
Taylor & Francis	Taylor & Francis, 1, 1.28% Taylor & Francis 1 publication, 1.28%
eLife Sciences Publications	eLife Sciences Publications, 1, 1.28% eLife Sciences Publications 1 publication, 1.28%
Cold Spring Harbor Laboratory	Cold Spring Harbor Laboratory, 1, 1.28% Cold Spring Harbor Laboratory 1 publication, 1.28%
	2 4 6 8 10 12 14 16 18

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GOST Copy

Polikanov Y. S. et al. Distinct tRNA Accommodation Intermediates Observed on the Ribosome with the Antibiotics Hygromycin A and A201A // Molecular Cell. 2015. Vol. 58. No. 5. pp. 832-844.

GOST all authors (up to 50) Copy

Polikanov Y. S., Starosta A. L., Juette M. F., Altman R. B., Terry D. S., Lu W., Burnett B. J., Dinos G. P., Reynolds K. R., Blanchard S., Steitz T. A., Wilson D. W. Distinct tRNA Accommodation Intermediates Observed on the Ribosome with the Antibiotics Hygromycin A and A201A // Molecular Cell. 2015. Vol. 58. No. 5. pp. 832-844.

RIS |

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RIS Copy

TY - JOUR

DO - 10.1016/j.molcel.2015.04.014

UR - https://doi.org/10.1016%2Fj.molcel.2015.04.014

TI - Distinct tRNA Accommodation Intermediates Observed on the Ribosome with the Antibiotics Hygromycin A and A201A

T2 - Molecular Cell

AU - Polikanov, Yury S

AU - Starosta, Agata L

AU - Juette, Manuel F

AU - Altman, Roger B

AU - Terry, Daniel S

AU - Lu, Wanli

AU - Burnett, Benjamin J

AU - Dinos, George P.

AU - Reynolds, Kevin R.

AU - Blanchard, Scott

AU - Steitz, Thomas A.

AU - Wilson, Daniel W.

PY - 2015

DA - 2015/06/01 00:00:00

PB - Elsevier

SP - 832-844

IS - 5

VL - 58

PMID - 26028538

SN - 1097-2765

SN - 1097-4164

ER -

BibTex |

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BibTex Copy

@article{2015_Polikanov,

author = {Yury S Polikanov and Agata L Starosta and Manuel F Juette and Roger B Altman and Daniel S Terry and Wanli Lu and Benjamin J Burnett and George P. Dinos and Kevin R. Reynolds and Scott Blanchard and Thomas A. Steitz and Daniel W. Wilson},

title = {Distinct tRNA Accommodation Intermediates Observed on the Ribosome with the Antibiotics Hygromycin A and A201A},

journal = {Molecular Cell},

year = {2015},

volume = {58},

publisher = {Elsevier},

month = {jun},

url = {https://doi.org/10.1016%2Fj.molcel.2015.04.014},

number = {5},

pages = {832--844},

doi = {10.1016/j.molcel.2015.04.014}

}

MLA

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MLA Copy

Polikanov, Yury S., et al. “Distinct tRNA Accommodation Intermediates Observed on the Ribosome with the Antibiotics Hygromycin A and A201A.” Molecular Cell, vol. 58, no. 5, Jun. 2015, pp. 832-844. https://doi.org/10.1016%2Fj.molcel.2015.04.014.

Found error?

Publisher

Elsevier

Journal

Molecular Cell

Quartile SCImago

Quartile WOS

Impact factor

ISSN

10972765 (Print)
10974164 (Electronic)