Accommodating the bacterial decoding release factor as an alien protein among the RNAs at the active site of the ribosome

Poole, Elizabeth S., Young, David J., Askarian-Amiri, Marjan E ., Scarlett, Debbie-Jane G. and Tate, Warren P. (2007) Accommodating the bacterial decoding release factor as an alien protein among the RNAs at the active site of the ribosome. Cell Research, 17 7: 591-607.


Author Poole, Elizabeth S.
Young, David J.
Askarian-Amiri, Marjan E .
Scarlett, Debbie-Jane G.
Tate, Warren P.
Title Accommodating the bacterial decoding release factor as an alien protein among the RNAs at the active site of the ribosome
Journal name Cell Research  (ERA 2012 Listed)    (ERA 2010 Rank B)   Check publisher's open access policy
Publication date 2007-07
Sub-type Review of research - research literature review (NOT book review
DOI 10.1038/cr.2007.56
Volume number 17
Issue number 7
ISSN 1001-0602; 1748-7838
Start page 591
End page 607
Total pages 17
Place of publication London, United Kingdom
Publisher Nature Publishing Group
Language eng
Abstract The decoding release factor (RF) triggers termination of protein synthesis by functionally mimicking a tRNA to span the decoding centre and the peptidyl transferase centre (PTC) of the ribosome. Structurally, it must fit into a site crafted for a tRNA and surrounded by five other RNAs, namely the adjacent peptidyl tRNA carrying the completed polypeptide, the mRNA and the three rRNAs. This is achieved by extending a structural domain from the body of the protein that results in a critical conformational change allowing it to contact the PTC. A structural model of the bacterial termination complex with the accommodated RF shows that it makes close contact with the first, second and third bases of the stop codon in the mRNA with two separate loops of structure: the anticodon loop and the loop at the tip of helix alpha5. The anticodon loop also makes contact with the base following the stop codon that is known to strongly influence termination efficiency. It confirms the close contact of domain 3 of the protein with the key RNA structures of the PTC. The mRNA signal for termination includes sequences upstream as well as downstream of the stop codon, and this may reflect structural restrictions for specific combinations of tRNA and RF to be bound onto the ribosome together. An unbiased SELEX approach has been investigated as a tool to identify potential rRNA-binding contacts of the bacterial RF in its different binding conformations within the active centre of the ribosome.
Keyword Release factor
Protein synthesis termination
tRNA
Functional mimicry
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Non-UQ

Document type: Journal Article
Sub-type: Review of research - research literature review (NOT book review
Collections: Excellence in Research Australia (ERA) - Collection
ERA 2012 Admin Only
Institute for Molecular Bioscience - Publications
 
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