| Amino-acid-dependent shift in tRNA synthetase editing mechanisms. | |
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MedLine Citation:
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PMID: 22017352 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Many aminoacyl-tRNA synthetases prevent mistranslation by relying upon proofreading activities at multiple stages of the aminoacylation reaction. In leucyl-tRNA synthetase (LeuRS), editing activities that precede or are subsequent to tRNA charging have been identified. Although both are operational, either the pre- or post-transfer editing activity can predominate. Yeast cytoplasmic LeuRS (ycLeuRS) misactivates structurally similar noncognate amino acids including isoleucine and methionine. We show that ycLeuRS has a robust post-transfer editing activity that efficiently clears tRNA(Leu) mischarged with isoleucine. In comparison, the enzyme's post-transfer hydrolytic activity against tRNA(Leu) mischarged with methionine is weak. Rather, methionyl-adenylate is cleared robustly via an enzyme-mediated pre-transfer editing activity. We hypothesize that, similar to E. coli LeuRS, ycLeuRS has coexisting functional pre- and post-transfer editing activities. In the case of ycLeuRS, a shift between the two editing pathways is triggered by the identity of the noncognate amino acid. |
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Authors:
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Jaya Sarkar; Susan A Martinis |
Publication Detail:
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Type: Journal Article; Research Support, N.I.H., Extramural Date: 2011-10-31 |
Journal Detail:
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Title: Journal of the American Chemical Society Volume: 133 ISSN: 1520-5126 ISO Abbreviation: J. Am. Chem. Soc. Publication Date: 2011 Nov |
Date Detail:
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Created Date: 2011-11-17 Completed Date: 2012-03-12 Revised Date: 2013-02-19 |
Medline Journal Info:
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Nlm Unique ID: 7503056 Medline TA: J Am Chem Soc Country: United States |
Other Details:
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Languages: eng Pagination: 18510-3 Citation Subset: IM |
Affiliation:
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Department of Biochemistry, University of Illinois at Urbana-Champaign, 419 Roger Adams Laboratory, Box B-4, 600 South Mathews Avenue, Urbana, Illinois 61801, USA. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Amino Acids*
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genetics,
metabolism Amino Acyl-tRNA Synthetases / chemistry, genetics, metabolism* Escherichia coli / enzymology RNA, Transfer, Leu* Yeasts / enzymology |
| Grant Support | |
ID/Acronym/Agency:
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GM063789/GM/NIGMS NIH HHS; R01 GM063789-07S1/GM/NIGMS NIH HHS; R01 GM063789-08/GM/NIGMS NIH HHS; R01 GM063789-09/GM/NIGMS NIH HHS; R01 GM063789-10/GM/NIGMS NIH HHS |
| Chemical | |
Reg. No./Substance:
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0/Amino Acids; 0/RNA, Transfer, Leu; EC 6.1.1.-/Amino Acyl-tRNA Synthetases |
| Comments/Corrections | |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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