Open Access
Cell Chemical Biology, volume 25, issue 12, pages 1506-1518.e13
Tetracyclines Modify Translation by Targeting Key Human rRNA Substructures
Mortison Jonathan D
1
,
Schenone Mónica
2
,
Myers Jacob A.
1
,
Zhang Ziyang
1
,
Chen Linfeng
1
,
Ciarlo Christie
2
,
Comer Eamon
2
,
Natchiar S. Kundhavai
3
,
Carr Steven
2
,
Klaholz B.P.
3
,
Myers Andrew T.
1
1
Dept. of Chemistry and Chemical Biology, Harvard University, Cambridge, MA 02138, USA.
|
3
Centre for Integrative Biology (CBI), Department of Integrated Structural Biology, IGBMC (Institute of Genetics and of Molecular and Cellular Biology), 1 Rue Laurent Fries, Illkirch 67404, France
|
Publication type: Journal Article
Publication date: 2018-12-01
Journal:
Cell Chemical Biology
Quartile SCImago
Q1
Quartile WOS
Q1
Impact factor: 8.6
ISSN: 24519448, 24519456
PubMed ID:
30318461
Drug Discovery
Biochemistry
Molecular Biology
Pharmacology
Clinical Biochemistry
Molecular Medicine
Abstract
Apart from their antimicrobial properties, tetracyclines demonstrate clinically validated effects in the amelioration of pathological inflammation and human cancer. Delineation of the target(s) and mechanism(s) responsible for these effects, however, has remained elusive. Here, employing quantitative mass spectrometry-based proteomics, we identified human 80S ribosomes as targets of the tetracyclines Col-3 and doxycycline. We then developed in-cell click selective crosslinking with RNA sequence profiling (icCL-seq) to map binding sites for these tetracyclines on key human rRNA substructures at nucleotide resolution. Importantly, we found that structurally and phenotypically variant tetracycline analogs could chemically discriminate these rRNA binding sites. We also found that tetracyclines both subtly modify human ribosomal translation and selectively activate the cellular integrated stress response (ISR). Together, the data reveal that targeting of specific rRNA substructures, activation of the ISR, and inhibition of translation are correlated with the anti-proliferative properties of tetracyclines in human cancer cell lines.
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- We do not take into account publications that without a DOI.
- Statistics recalculated only for publications connected to researchers, organizations and labs registered on the platform.
- Statistics recalculated weekly.
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GOST
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Mortison J. D. et al. Tetracyclines Modify Translation by Targeting Key Human rRNA Substructures // Cell Chemical Biology. 2018. Vol. 25. No. 12. p. 1506-1518.e13.
GOST all authors (up to 50)
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Mortison J. D., Schenone M., Myers J. A., Zhang Z., Chen L., Ciarlo C., Comer E., Natchiar S. K., Carr S., Klaholz B., Myers A. T. Tetracyclines Modify Translation by Targeting Key Human rRNA Substructures // Cell Chemical Biology. 2018. Vol. 25. No. 12. p. 1506-1518.e13.
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RIS
Copy
TY - JOUR
DO - 10.1016/j.chembiol.2018.09.010
UR - https://doi.org/10.1016%2Fj.chembiol.2018.09.010
TI - Tetracyclines Modify Translation by Targeting Key Human rRNA Substructures
T2 - Cell Chemical Biology
AU - Mortison, Jonathan D
AU - Schenone, Mónica
AU - Myers, Jacob A.
AU - Zhang, Ziyang
AU - Chen, Linfeng
AU - Ciarlo, Christie
AU - Comer, Eamon
AU - Natchiar, S. Kundhavai
AU - Carr, Steven
AU - Klaholz, B.P.
AU - Myers, Andrew T.
PY - 2018
DA - 2018/12/01 00:00:00
PB - Elsevier
SP - 1506-1518.e13
IS - 12
VL - 25
PMID - 30318461
SN - 2451-9448
SN - 2451-9456
ER -
Cite this
BibTex
Copy
@article{2018_Mortison,
author = {Jonathan D Mortison and Mónica Schenone and Jacob A. Myers and Ziyang Zhang and Linfeng Chen and Christie Ciarlo and Eamon Comer and S. Kundhavai Natchiar and Steven Carr and B.P. Klaholz and Andrew T. Myers},
title = {Tetracyclines Modify Translation by Targeting Key Human rRNA Substructures},
journal = {Cell Chemical Biology},
year = {2018},
volume = {25},
publisher = {Elsevier},
month = {dec},
url = {https://doi.org/10.1016%2Fj.chembiol.2018.09.010},
number = {12},
pages = {1506--1518.e13},
doi = {10.1016/j.chembiol.2018.09.010}
}
Cite this
MLA
Copy
Mortison, Jonathan D., et al. “Tetracyclines Modify Translation by Targeting Key Human rRNA Substructures.” Cell Chemical Biology, vol. 25, no. 12, Dec. 2018, pp. 1506-1518.e13. https://doi.org/10.1016%2Fj.chembiol.2018.09.010.