| β-Lysine discrimination by lysyl-tRNA synthetase. | |
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MedLine Citation:
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PMID: 21925499 Owner: NLM Status: Publisher |
Abstract/OtherAbstract:
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Elongation factor P is modified with (R)-β-lysine by the lysyl-tRNA synthetase (LysRS) paralog PoxA. PoxA specificity is orthogonal to LysRS, despite their high similarity. To investigate α- and β-lysine recognition by LysRS and PoxA, amino acid replacements were made in the LysRS active site guided by the PoxA structure. A233S LysRS behaved as wild type with α-lysine, while the G469A and A233S/G469A variants decreased stable α-lysyl-adenylate formation. A233S LysRS recognized β-lysine better than wildtype, suggesting a role for this residue in discriminating α- and β-amino acids. Both enantiomers of β-lysine were substrates for tRNA aminoacylation by LysRS, which, together with the relaxed specificity of the A233S variant, suggest a possible means to develop systems for in vivo co-translational insertion of β-amino acids. |
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Authors:
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Marla S Gilreath; Hervé Roy; Tammy J Bullwinkle; Assaf Katz; William W Navarre; Michael Ibba |
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Publication Detail:
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Type: JOURNAL ARTICLE Date: 2011-9-12 |
Journal Detail:
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Title: FEBS letters Volume: - ISSN: 1873-3468 ISO Abbreviation: - Publication Date: 2011 Sep |
Date Detail:
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Created Date: 2011-9-19 Completed Date: - Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 0155157 Medline TA: FEBS Lett Country: - |
Other Details:
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Languages: ENG Pagination: - Citation Subset: - |
Copyright Information:
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Copyright © 2011. Published by Elsevier B.V. |
Affiliation:
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Ohio State Biochemistry Program, Center for RNA Biology, Ohio State University, Columbus, OH 43210, USA. |
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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