| Post-transfer editing in vitro and in vivo by the beta subunit of phenylalanyl-tRNA synthetase. | |
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MedLine Citation:
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PMID: 15526031 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Translation of the genetic code requires attachment of tRNAs to their cognate amino acids. Errors during amino-acid activation and tRNA esterification are corrected by aminoacyl-tRNA synthetase-catalyzed editing reactions, as extensively described for aliphatic amino acids. The contribution of editing to aromatic amino-acid discrimination is less well understood. We show that phenylalanyl-tRNA synthetase misactivates tyrosine and that it subsequently corrects such errors through hydrolysis of tyrosyl-adenylate and Tyr-tRNA(Phe). Structural modeling combined with an in vivo genetic screen identified the editing site in the B3/B4 domain of the beta subunit, 40 angstroms from the active site in the alpha subunit. Replacements of residues within the editing site had no effect on Phe-tRNA(Phe) synthesis, but abolished hydrolysis of Tyr-tRNA(Phe) in vitro. Expression of the corresponding mutants in Escherichia coli significantly slowed growth, and changed the activity of a recoded beta-galactosidase variant by misincorporating tyrosine in place of phenylalanine. This loss in aromatic amino-acid discrimination in vivo revealed that editing by phenylalanyl-tRNA synthetase is essential for faithful translation of the genetic code. |
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Authors:
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Hervé Roy; Jiqiang Ling; Michael Irnov; Michael Ibba |
Publication Detail:
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Type: Journal Article; Research Support, U.S. Gov't, Non-P.H.S. Date: 2004-11-04 |
Journal Detail:
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Title: The EMBO journal Volume: 23 ISSN: 0261-4189 ISO Abbreviation: EMBO J. Publication Date: 2004 Nov |
Date Detail:
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Created Date: 2004-11-24 Completed Date: 2005-06-28 Revised Date: 2013-04-18 |
Medline Journal Info:
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Nlm Unique ID: 8208664 Medline TA: EMBO J Country: England |
Other Details:
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Languages: eng Pagination: 4639-48 Citation Subset: IM |
Affiliation:
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Department of Microbiology, The Ohio State University, Columbus, OH 43210-1292, USA. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Escherichia coli
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enzymology*,
genetics Hydrolysis Models, Molecular Mutation Phenylalanine / metabolism Phenylalanine-tRNA Ligase / genetics, metabolism* Plasmids Protein Biosynthesis* Protein Subunits / genetics, metabolism RNA, Transfer, Phe / genetics, metabolism Tyrosine / metabolism Tyrosine-tRNA Ligase / genetics, metabolism |
| Chemical | |
Reg. No./Substance:
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0/Protein Subunits; 0/RNA, Transfer, Phe; 55520-40-6/Tyrosine; 63-91-2/Phenylalanine; EC 6.1.1.1/Tyrosine-tRNA Ligase; EC 6.1.1.20/Phenylalanine-tRNA Ligase |
| Comments/Corrections | |
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