Abstract
The function of SmpB protein in the trans-translation system was evaluated using the well-defined cell-free translation system consisting of purified ribosome, alanyl-tRNA synthetase and elongation factors. The analysis showed that SmpB protein enhances alanine-accepting activity of tmRNA and that SmpB protein and tmRNA are sufficient to complete the trans-translation process in the presence of translational components. Moreover, SmpB is indispensable in the addition of tag-peptide onto ribosomes by tmRNA. In particular, the A-site binding of tmRNA is inhibited in the absence of SmpB.
Original language | English |
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Pages (from-to) | 74-77 |
Number of pages | 4 |
Journal | FEBS Letters |
Volume | 514 |
Issue number | 1 |
DOIs | |
Publication status | Published - 2002 Mar 6 |
Externally published | Yes |
Keywords
- 10Sa
- SmpB
- SsrA
- Translation
- tmRNA
- trans-Translation
ASJC Scopus subject areas
- Biophysics
- Structural Biology
- Biochemistry
- Molecular Biology
- Genetics
- Cell Biology