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• W2021330803 endingPage "1425" @default.
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• W2021330803 abstract "Elongation factor G (EF-G) promotes the translocation of tRNA and mRNA in the central cavity of the ribosome following the addition of each amino acid residue to a growing polypeptide chain. tRNA/mRNA translocation is coupled to GTP hydrolysis, catalyzed by EF-G and activated by the ribosome. In this study we probed EF-G interactions with ribosomal proteins (r-proteins) of the bacterial ribosome, by using a combination of chemical crosslinking, immunoblotting and mass spectroscopy analyses. We identified three bacterial r-proteins (L7/L12, S12 and L6) crosslinked to specific residues of EF-G in three of its domains (G′, 3 and 5, respectively). EF-G crosslinks to L7/L12 and S12 were indistinguishable when EF-G was trapped on the ribosome before or after tRNA/mRNA translocation had occurred, whereas a crosslink between EF-G and L6 formed with greater efficiency before translocation had occurred. EF-G crosslinked to L7/L12 was capable of catalyzing multiple rounds of GTP hydrolysis, whereas EF-G crosslinked to S12 was inactive in GTP hydrolysis. These results imply that during the GTP hydrolytic cycle EF-G must detach from S12 within the central cavity of the ribosome, while EF-G can remain associated with L7/L12 located on one of the peripheral stalks of the ribosome. This mechanism may ensure that a single GTP molecule is hydrolyzed for each tRNA/mRNA translocation event." @default.
• W2021330803 created "2016-06-24" @default.
• W2021330803 creator A5058323167 @default.
• W2021330803 creator A5065331535 @default.
• W2021330803 date "2007-05-01" @default.
• W2021330803 modified "2023-09-26" @default.
• W2021330803 title "Crosslinking of Translation Factor EF-G to Proteins of the Bacterial Ribosome Before and After Translocation" @default.
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• W2021330803 doi "https://doi.org/10.1016/j.jmb.2007.03.009" @default.
• W2021330803 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/17395204" @default.
• W2021330803 hasPublicationYear "2007" @default.
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