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tmRNA-SmpB complex ...
tmRNA-SmpB complex mimics native aminoacyl-tRNAs in the A site of stalled ribosomes
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- Cheng, Kimberley (author)
- Karolinska Institutet,KTH,Strukturell bioteknik
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- Ivanova, Natalia (author)
- Uppsala universitet,Institutionen för cell- och molekylärbiologi,ehrenberg
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- Scheres, Sjores (author)
- CSIC, Natl Biotechnol Ctr, Biocomp Unit, E-28049 Madrid, Spain
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- Pavlov, Michael Y (author)
- Uppsala universitet,Institutionen för cell- och molekylärbiologi,ehrenberg
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- Maria Carazo, Jose (author)
- Lund Univ, Mol Biophys KILU
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- Hebert, Hans (author)
- Karolinska Institutet,KTH,Strukturell bioteknik
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- Ehrenberg, Måns (author)
- Uppsala universitet,Institutionen för cell- och molekylärbiologi
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- Lindahl, Martin (author)
- Lund University,Lunds universitet,KTH,Strukturell bioteknik,Biokemi och Strukturbiologi,Centrum för Molekylär Proteinvetenskap,Kemiska institutionen,Institutioner vid LTH,Lunds Tekniska Högskola,Biochemistry and Structural Biology,Center for Molecular Protein Science,Department of Chemistry,Departments at LTH,Faculty of Engineering, LTH
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(creator_code:org_t)
- Elsevier BV, 2010
- 2010
- English.
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In: Journal of Structural Biology. - : Elsevier BV. - 1047-8477 .- 1095-8657. ; 169:3, s. 342-348
- Related links:
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Abstract
Subject headings
Close
- Bacterial ribosomes stalled on faulty, often truncated, mRNAs lacking stop codons are rescued by trans-translation. It relies on an RNA molecule (tmRNA) capable of replacing the faulty mRNA with its own open reading frame (ORF). Translation of tmRNA ORF results in the tagging of faulty protein for degradation and its release from the ribosome. We used single-particle cryo-electron microscopy to visualize tmRNA together with its helper protein SmpB on the 70S Escherichia coli ribosome in states subsequent to GTP hydrolysis on elongation factor Tu (EF-Tu). Three-dimensional reconstruction and heterogeneity analysis resulted in a 15 A resolution structure of the tmRNA-SmpB complex accommodated in the A site of the ribosome, which shows that SmpB mimics the anticodon- and D-stem of native tRNAs missing in the tRNA-like domain of tmRNA. We conclude that the tmRNA-SmpB complex accommodates in the ribosomal A site very much like an aminoacyl-tRNA during protein elongation.
Subject headings
- TEKNIK OCH TEKNOLOGIER -- Industriell bioteknik (hsv//swe)
- ENGINEERING AND TECHNOLOGY -- Industrial Biotechnology (hsv//eng)
- NATURVETENSKAP -- Biologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences (hsv//eng)
Keyword
- Trans-translation
- tmRNA
- SmpB
- Cryo-electron microscopy
- Single-particle
- Heterogeneity analysis
- Bioengineering
- Bioteknik
- tmRNA
- Trans-translation
- SmpB
- Cryo-electron microscopy
- Single-particle
- Heterogeneity analysis
Publication and Content Type
- ref (subject category)
- art (subject category)
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