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  The antibiotic kasugamycin mimics mRNA nucleotides to destabilize tRNA binding and inhibit canonical translation initiation

Schluenzen, F., Takemoto, C., Wilson, D. N., Kaminishi, T., Harms, J. M.., Hanawa-Suetsugu, K., et al. (2006). The antibiotic kasugamycin mimics mRNA nucleotides to destabilize tRNA binding and inhibit canonical translation initiation. Nature Structural & Molecular Biology, 13, 871-878. doi:10.1038/nsmb1145.

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Genre: Journal Article
Alternative Title : Nat. Struct. Mol. Biol.

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 Creators:
Schluenzen, Frank1, Author
Takemoto, Chie, Author
Wilson, Daniel N1, Author
Kaminishi, Tatsuya, Author
Harms, Joerg M .1, Author
Hanawa-Suetsugu, Kyoko, Author
Szaflarski, Witold2, Author           
Kawazoe, Masahito, Author
Shirouzu, Mikako, Author
Nierhaus, Knud2, Author           
Yokoyama, Shigeyuki, Author
Fucini, Paola2, Author           
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1Max Planck Society, ou_persistent13              
2Ribosomes, Max Planck Institute for Molecular Genetics, Max Planck Society, ou_1433558              

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 Abstract: Kasugamycin (Ksg) specifically inhibits translation initiation of canonical but not of leaderless messenger RNAs. Ksg inhibition is thought to occur by direct competition with initiator transfer RNA. The 3.35-Å structure of Ksg bound to the 30S ribosomal subunit presented here provides a structural description of two Ksg-binding sites as well as a basis for understanding Ksg resistance. Notably, neither binding position overlaps with P-site tRNA; instead, Ksg mimics codon nucleotides at the P and E sites by binding within the path of the mRNA. Coupled with biochemical experiments, our results suggest that Ksg indirectly inhibits P-site tRNA binding through perturbation of the mRNA-tRNA codon-anticodon interaction during 30S canonical initiation. In contrast, for 70S-type initiation on leaderless mRNA, the overlap between mRNA and Ksg is reduced and the binding of tRNA is further stabilized by the presence of the 50S subunit, minimizing Ksg efficacy.

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Language(s): eng - English
 Dates: 2006-09-24
 Publication Status: Issued
 Pages: -
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 Identifiers: eDoc: 305623
DOI: 10.1038/nsmb1145
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Title: Nature Structural & Molecular Biology
  Alternative Title : Nat. Struct. Mol. Biol.
Source Genre: Journal
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Pages: - Volume / Issue: 13 Sequence Number: - Start / End Page: 871 - 878 Identifier: ISSN: 1545-9993