Journal
NATURE STRUCTURAL & MOLECULAR BIOLOGY
Volume 14, Issue 6, Pages 493-497Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/nsmb1243
Keywords
-
Funding
- NCRR NIH HHS [5P41RR03155] Funding Source: Medline
- NIGMS NIH HHS [GM-17129] Funding Source: Medline
Ask authors/readers for more resources
During protein synthesis, transfer RNA and messenger RNA undergo coupled translocation through the ribosome's A, P and E sites, a process catalyzed by elongation factor EF-G. Viomycin blocks translocation on bacterial ribosomes and is believed to bind at the subunit interface. Using fluorescent resonance energy transfer and chemical footprinting, we show that viomycin traps the ribosome in an intermediate state of translocation. Changes in FRET efficiency show that viomycin causes relative movement of the two ribosomal subunits indistinguishable from that induced by binding of EF-G with GDPNP. Chemical probing experiments indicate that viomycin induces formation of a hybrid-state translocation intermediate. Thus, viomycin inhibits translation through a unique mechanism, locking ribosomes in the hybrid state; the EF-G- induced 'ratcheted' state observed by cryo-EM is identical to the hybrid state; and, since translation is viomycin sensitive, the hybrid state may be present in vivo.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available