2007年12月
Interaction of SmpB with ribosome from directed hydroxyl radical probing
NUCLEIC ACIDS RESEARCH
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- ,
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- 巻
- 35
- 号
- 21
- 開始ページ
- 7248
- 終了ページ
- 7255
- 記述言語
- 英語
- 掲載種別
- DOI
- 10.1093/nar/gkm677
- 出版者・発行元
- OXFORD UNIV PRESS
To add a tag-peptide for degradation to the nascent polypeptide in a stalled ribosome, an unusual translation called trans-translation is facilitated by transfer-messenger RNA (tmRNA) having an upper half of the tRNA structure and the sequence encoding the tag-peptide except the first alanine. During this event, tmRNA enters the vacant A-site of the stalled ribosome without a codonanticodon interaction, but with a protein factor SmpB. Here, we studied the sites and modes of binding of SmpB to the ribosome by directed hydroxyl radical probing from Fe(II) tethered to SmpB variants. It revealed two SmpB-binding sites, A-site and P-site, on the ribosome. Each SmpB can be superimposed on the lower half of tRNA behaving in translation. The sites of cleavages from Fe(II) tethered to the C-terminal residues of A-site SmpB are aligned along the mRNA path towards the downstream tunnel, while those of P-site SmpB are found almost exclusively around the region of the codonanticodon interaction in the P-site. We propose a new model of trans-translation in that the C-terminal tail of SmpB initially recognizes the decoding region and the mRNA path free of mRNA by mimicking mRNA.
- リンク情報
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- DOI
- https://doi.org/10.1093/nar/gkm677
- CiNii Articles
- http://ci.nii.ac.jp/naid/80017997876
- PubMed
- https://www.ncbi.nlm.nih.gov/pubmed/17959652
- Web of Science
- https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:000251868800029&DestApp=WOS_CPL
- ID情報
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- DOI : 10.1093/nar/gkm677
- ISSN : 0305-1048
- CiNii Articles ID : 80017997876
- PubMed ID : 17959652
- Web of Science ID : WOS:000251868800029