de.mpg.escidoc.pubman.appbase.FacesBean
English
 
Help Guide Disclaimer Contact us Login
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT

Released

Journal Article

Codon-Anticodon Interaction at the P Site Is a Prerequisite for tRNA Interaction with the Small Ribosomal Subunit

MPS-Authors

Schäfer,  Markus A.
Max Planck Society;

Tastan,  A. Özlem
Max Planck Society;

Patzke,  Sebastian
Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons50104

Blaha,  Gregor
Ribosomes, Max Planck Institute for Molecular Genetics, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons50563

Spahn,  Christian M. T.
Dept. of Vertebrate Genomics (Head: Hans Lehrach), Max Planck Institute for Molecular Genetics, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons50642

Wilson,  Daniel N.
Dept. of Vertebrate Genomics (Head: Hans Lehrach), Max Planck Institute for Molecular Genetics, Max Planck Society;

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

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

Locator
There are no locators available
Fulltext (public)
There are no public fulltexts available
Supplementary Material (public)
There is no public supplementary material available
Citation

Schäfer, M. A., Tastan, A. Ö., Patzke, S., Blaha, G., Spahn, C. M. T., Wilson, D. N., et al. (2002). Codon-Anticodon Interaction at the P Site Is a Prerequisite for tRNA Interaction with the Small Ribosomal Subunit. Journal of Biological Chemistry, 277(21), 19095-19105.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0010-8C48-9
Abstract
The arrival of high resolution crystal structures for the ribosomal subunits opens a new phase of molecular analysis and asks for corresponding analyses of ribosomal function. Here we apply the phosphorothioate technique to dissect tRNA interactions with the ribosome. We demonstrate that a tRNA bound to the P site of non-programmed 70 S ribosomes contacts predominantly the 50 S, as opposed to the 30 S subunit, indicating that codon-anticodon interaction at the P site is a prerequisite for 30 S binding. Protection patterns of tRNAs bound to isolated subunits and programmed 70 S ribosomes were compared. The results suggest the presence of a movable domain in the large ribosomal subunit that carries tRNA and reveal that only ~15% of a tRNA, namely residues 30 ± 1 to 43 ± 1, contact the 30 S subunit of programmed 70 S ribosomes, whereas the remaining 85% make contact with the 50 S subunit. Identical protection patterns of two distinct elongator tRNAs at the P site were identified as tRNA species-independent phosphate backbone contacts. The sites of protection correlate nicely with the predicted ribosomal-tRNA contacts deduced from a 5.5-Å crystal structure of a programmed 70 S ribosome, thus refining which ribosomal components are critical for tRNA fixation at the P site.