aaRSs (aminoacyl-tRNA synthetases) establish the rules of the genetic code by catalysing the formation of aminoacyl-tRNA. The quality control for aminoacylation is achieved by editing activity, which is usually carried out by a discrete editing domain. For LeuRS (leucyl-tRNA synthetase), the CP1 (connective peptide 1) domain is the editing domain responsible for hydrolysing mischarged tRNA. The CP1 domain is universally present in LeuRSs, except MmLeuRS (Mycoplasma mobile LeuRS). The substitute of CP1 in MmLeuRS is a nonapeptide (MmLinker). In the present study, we show that the MmLinker, which is critical for the aminoacylation activity of MmLeuRS, could confer remarkable tRNA-charging activity on the inactive CP1-deleted LeuRS from Escherichia coli (EcLeuRS) and Aquifex aeolicus (AaLeuRS). Furthermore, CP1 from EcLeuRS could functionally compensate for the MmLinker and endow MmLeuRS with post-transfer editing capability. These investigations provide a mechanistic framework for the modular construction of aaRSs and their co-ordination to achieve catalytic efficiency and fidelity. These results also show that the pre-transfer editing function of LeuRS originates from its conserved synthetic domain and shed light on future study of the mechanism.
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Research Article|
March 27 2012
A naturally occurring nonapeptide functionally compensates for the CP1 domain of leucyl-tRNA synthetase to modulate aminoacylation activity
Min Tan;
Min Tan
1
1State Key Laboratory of Molecular Biology, Center for RNA Research, Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences, The Chinese Academy of Sciences, 320 Yue Yang Road, Shanghai 200031, China
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Wei Yan;
Wei Yan
1
1State Key Laboratory of Molecular Biology, Center for RNA Research, Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences, The Chinese Academy of Sciences, 320 Yue Yang Road, Shanghai 200031, China
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Ru-Juan Liu;
Ru-Juan Liu
1State Key Laboratory of Molecular Biology, Center for RNA Research, Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences, The Chinese Academy of Sciences, 320 Yue Yang Road, Shanghai 200031, China
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Meng Wang;
Meng Wang
1State Key Laboratory of Molecular Biology, Center for RNA Research, Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences, The Chinese Academy of Sciences, 320 Yue Yang Road, Shanghai 200031, China
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Xin Chen;
Xin Chen
1State Key Laboratory of Molecular Biology, Center for RNA Research, Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences, The Chinese Academy of Sciences, 320 Yue Yang Road, Shanghai 200031, China
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Xiao-Long Zhou;
Xiao-Long Zhou
1State Key Laboratory of Molecular Biology, Center for RNA Research, Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences, The Chinese Academy of Sciences, 320 Yue Yang Road, Shanghai 200031, China
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En-Duo Wang
En-Duo Wang
2
1State Key Laboratory of Molecular Biology, Center for RNA Research, Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences, The Chinese Academy of Sciences, 320 Yue Yang Road, Shanghai 200031, China
2To whom correspondence should be addressed (email [email protected]).
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Publisher: Portland Press Ltd
Received:
October 28 2011
Revision Received:
January 31 2012
Accepted:
February 01 2012
Accepted Manuscript online:
February 01 2012
Online ISSN: 1470-8728
Print ISSN: 0264-6021
© The Authors Journal compilation © 2012 Biochemical Society
2012
Biochem J (2012) 443 (2): 477–484.
Article history
Received:
October 28 2011
Revision Received:
January 31 2012
Accepted:
February 01 2012
Accepted Manuscript online:
February 01 2012
Citation
Min Tan, Wei Yan, Ru-Juan Liu, Meng Wang, Xin Chen, Xiao-Long Zhou, En-Duo Wang; A naturally occurring nonapeptide functionally compensates for the CP1 domain of leucyl-tRNA synthetase to modulate aminoacylation activity. Biochem J 15 April 2012; 443 (2): 477–484. doi: https://doi.org/10.1042/BJ20111925
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