New Study Reveals a Novel Quality Control Mechanism by Leucyl-tRNA Synthetase
Source:
Time: 2012-12-29
Aminoacyl-tRNA synthetases (aaRSs) catalyze the attachment of amino acids to their cognate tRNAs with amino acids for protein biosynthesis. Editing function, which eliminate the mis-activated amino acid or mis-aminoacylated products, is essential for the fidelity of aminoacylation and the subsequent accurate translation. Recently researchers from Chinese Academy of Sciences revealed a novel quality control mechanism by leucyl-tRNA synthetase from Escherichia coli (EcLeuRS).
Dr. Min Tan and his colleagues guided by Professor Enduo Wang from Shanghai Institute of Biochemistry and Cell Biology, Chinese Academy of Sciences found that there is inter-domain communication between the aminoacylation and editing domains of EcLeuRS. The key residues involving in the communication are characterized. The communication between the two domains modulates the activity of tRNA-dependent pre-transfer editing, then feedback inhibiting the formation of misactivated amino acids in the synthetic active site. These results also suggested a novel quality control mechanism of EcLeuRS obtained by the cooperation of synthetic and editing domains.
This work, entitled “Interdomain communication modulates the tRNA-dependent pre-transfer editing of leucyl-tRNA synthetase”, was published in Biochemical Journal. This work was funded by National Natural Science Foundation of China, Ministry of Science and Technology and Chinese Academy of Science.
AUTHOR CONTACT:
WANG Enduo
Shanghai Institute of Biochemistry and Cell Biology, Chinese Academy of Sciences, Shanghai, China
Tertiary orientation and sequence alignment of the residues investigated in this research (Image provided by Prof. WANG Enduo)
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