Open Access
Open access
Science, volume 336, issue 6083, pages 915-918

How Hibernation Factors RMF, HPF, and YfiA Turn Off Protein Synthesis

Polikanov Yury S. 1, 2
Blaha Gregor M 1
Steitz Thomas A. 1, 2, 3
1
 
Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520–8114, USA.
2
 
Howard Hughes Medical Institute, Yale University, New Haven, CT 06520–8114, USA.
3
 
Department of Chemistry, Yale University, New Haven, CT 06520–8114, USA.
Publication typeJournal Article
Publication date2012-05-17
Journal: Science
Quartile SCImago
Q1
Quartile WOS
Q1
Impact factor56.9
ISSN00368075, 10959203
Multidisciplinary
Abstract
The Hibernating Ribosome When bacteria enter stationary phase, their ribosomes are inactivated. In Escherichia coli, ribosome modulation factor (RMF) causes dimerization of the 70S ribosome and the dimer is stabilized by, hibernation promotion factor (HPF). Alternately, the stationary phase protein, YfiA, inactivates 70S ribosomes. Polikanov et al. (p. 915) present high-resolution structures of the Thermus thermophilus 70S ribosome bound to each of these three factors. The structures suggest that RMF binding inhibits protein synthesis by preventing initial messenger RNA (mRNA) binding and that HPF and YfiA have overlapping binding sites and would both interfere with binding of mRNA, transfer RNA, and initiation factors. Three crystal structures show why bacteria stop making proteins when they enter the stationary phase. Eubacteria inactivate their ribosomes as 100S dimers or 70S monomers upon entry into stationary phase. In Escherichia coli, 100S dimer formation is mediated by ribosome modulation factor (RMF) and hibernation promoting factor (HPF), or alternatively, the YfiA protein inactivates ribosomes as 70S monomers. Here, we present high-resolution crystal structures of the Thermus thermophilus 70S ribosome in complex with each of these stationary-phase factors. The binding site of RMF overlaps with that of the messenger RNA (mRNA) Shine-Dalgarno sequence, which prevents the interaction between the mRNA and the 16S ribosomal RNA. The nearly identical binding sites of HPF and YfiA overlap with those of the mRNA, transfer RNA, and initiation factors, which prevents translation initiation. The binding of RMF and HPF, but not YfiA, to the ribosome induces a conformational change of the 30S head domain that promotes 100S dimer formation.

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GOST |
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GOST Copy
Polikanov Y. S. et al. How Hibernation Factors RMF, HPF, and YfiA Turn Off Protein Synthesis // Science. 2012. Vol. 336. No. 6083. pp. 915-918.
GOST all authors (up to 50) Copy
Polikanov Y. S., Blaha G. M., Steitz T. A. How Hibernation Factors RMF, HPF, and YfiA Turn Off Protein Synthesis // Science. 2012. Vol. 336. No. 6083. pp. 915-918.
RIS |
Cite this
RIS Copy
TY - JOUR
DO - 10.1126/science.1218538
UR - https://doi.org/10.1126%2Fscience.1218538
TI - How Hibernation Factors RMF, HPF, and YfiA Turn Off Protein Synthesis
T2 - Science
AU - Polikanov, Yury S.
AU - Blaha, Gregor M
AU - Steitz, Thomas A.
PY - 2012
DA - 2012/05/17 00:00:00
PB - American Association for the Advancement of Science (AAAS)
SP - 915-918
IS - 6083
VL - 336
PMID - 22605777
SN - 0036-8075
SN - 1095-9203
ER -
BibTex |
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BibTex Copy
@article{2012_Polikanov
author = {Yury S. Polikanov and Gregor M Blaha and Thomas A. Steitz},
title = {How Hibernation Factors RMF, HPF, and YfiA Turn Off Protein Synthesis},
journal = {Science},
year = {2012},
volume = {336},
publisher = {American Association for the Advancement of Science (AAAS)},
month = {may},
url = {https://doi.org/10.1126%2Fscience.1218538},
number = {6083},
pages = {915--918},
doi = {10.1126/science.1218538}
}
MLA
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MLA Copy
Polikanov, Yury S., et al. “How Hibernation Factors RMF, HPF, and YfiA Turn Off Protein Synthesis.” Science, vol. 336, no. 6083, May. 2012, pp. 915-918. https://doi.org/10.1126%2Fscience.1218538.
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