Document Detail


Inter-domain communication modulates the tRNA-dependent pre-transfer editing of leucyl-tRNA synthetase.
MedLine Citation:
PMID:  23035846     Owner:  NLM     Status:  Publisher    
Abstract/OtherAbstract:
Leucyl-tRNA synthetase from Escherichia coli (EcLeuRS) has evolved both tRNA-dependent pre- and post-transfer editing capabilities to ensure catalytic specificity. Both editing functions rely on entry of the tRNA CCA tail into the editing domain of the LeuRS enzyme, which, according to X-ray crystal structural studies, leads to a dynamic, disordered orientation of the interface between the synthetic and editing domains. Here, our results show that this tRNA-triggered conformational rearrangement leads to inter-domain communication between the editing and synthetic domains through their interface, and this communication mechanism modulates the activity of tRNA-dependent pre-transfer editing. Furthermore, the tRNA-dependent editing reaction inhibits misactivation of noncognate amino acids from the synthetic active site. These results also suggest a novel quality control mechanism of EcLeuRS, which is achieved through the coordination between synthetic and editing domains.
Authors:
Min Tan; Bin Zhu; Ru-Juan Liu; Xin Chen; Xiao-Long Zhou; En-Duo Wang
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Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2012-10-4
Journal Detail:
Title:  The Biochemical journal     Volume:  -     ISSN:  1470-8728     ISO Abbreviation:  Biochem. J.     Publication Date:  2012 Oct 
Date Detail:
Created Date:  2012-10-5     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  2984726R     Medline TA:  Biochem J     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
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