Structure of a hibernating 100S ribosome reveals an inactive conformation of the ribosomal protein S1
Author:
Publisher
Springer Science and Business Media LLC
Subject
Cell Biology,Microbiology (medical),Genetics,Applied Microbiology and Biotechnology,Immunology,Microbiology
Link
http://www.nature.com/articles/s41564-018-0237-0.pdf
Reference49 articles.
1. Gohara, D. W. & Yap, M. F. Survival of the drowsiest: the hibernating 100S ribosome in bacterial stress management. Curr. Genet. 64, 753–760 (2018).
2. Wada, A., Yamazaki, Y., Fujita, N. & Ishihama, A. Structure and probable genetic location of a ribosome modulation factor associated with 100S ribosomes in stationary-phase Escherichia coli cells. Proc. Natl Acad. Sci. USA 87, 2657–2661 (1990).
3. Maki, Y., Yoshida, H. & Wada, A. Two proteins, YfiA and YhbH, associated with resting ribosomes in stationary phase Escherichia coli. Genes Cells 5, 965–974 (2000).
4. Ueta, M. et al. Ribosome binding proteins YhbH and YfiA have opposite functions during 100S formation in the stationary phase of Escherichia coli. Genes Cells 10, 1103–1112 (2005).
5. Beckert, B. et al. Structure of the Bacillus subtilis hibernating 100S ribosome reveals the basis for 70S dimerization. EMBO J. 36, 2061–2072 (2017).
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