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Stepping tmRNA through the ribosome

MPG-Autoren
http://pubman.mpdl.mpg.de/cone/persons/resource/persons50444

Nierhaus,  Knud H.
Ribosomes, Max Planck Institute for Molecular Genetics, Max Planck Society;

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Zitation

Shpanchenko, O. V., Zvereva, M. I., Ivanov, P. V., Bugaeva, E. Y., Rozov, A. S., Bogdanov, A. A., et al. (2005). Stepping tmRNA through the ribosome. Journal of Biological Chemistry, 280(18), 18368-18374. doi:10.1074/jbc.M409094200.


Zitierlink: http://hdl.handle.net/11858/00-001M-0000-0010-864F-2
Zusammenfassung
tmRNA (transfer messenger RNA) is a unique molecule used by all bacteria to rescue stalled ribosomes and to mark unfinished peptides with a specific degradation signal. tmRNA is recruited by arrested ribosomes in which it facilitates the translational switch from cellular mRNA to the mRNA part of tmRNA. Small protein B (SmpB) is a key partner for the trans-translation activity of tmRNA both in vivo and in vitro. It was shown that SmpB acts at the initiation step of the trans-translation process by facilitating tmRNA aminoacylation and binding to the ribosome. Little is known about the subsequent steps of trans-translation. Here we demonstrated the first example of an investigation of tmRNA·ribosome complexes at different stages of trans-translation. Our results show that the structural element at the position of tmRNA pseudoknot 3 remains intact during the translation of the mRNA module of tmRNA and that it is localized on the surface of the ribosome. At least one SmpB molecule remains bound to a ribosome·tmRNA complex isolated from the cell when translation is blocked at different positions within the mRNA part of tmRNA.