Comment
doi: 10.1073/pnas.0402276101.
Epub 2004 May 11.
Turning tRNA upside down: When aminoacylation is not a prerequisite to protein synthesis
Affiliations
- PMID: 15138304
- PMCID: PMC419631
- DOI: 10.1073/pnas.0402276101
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Comment
Turning tRNA upside down: When aminoacylation is not a prerequisite to protein synthesis
Proc Natl Acad Sci U S A.
.
No abstract available
Figures
Pathways used by YadB and GluRS to attach glutamate to tRNA. YadB (upper pathway) first activates glutamate (Glu) in the absence of tRNA to yield glutamyl-adenylate (Glu-AMP) and pyrophosphate (PPi). Glu-AMP then serves as substrate for the attachment of glutamate to the Q-base at the first anticodon position of tRNAAsp. In contrast, GluRS (lower pathway) requires the presence of tRNAGlu for Glu-AMP synthesis and subsequently attaches glutamate to the 3′-terminal adenosine of tRNAGlu.
Comment on
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An aminoacyl-tRNA synthetase-like protein encoded by the Escherichia coli yadB gene glutamylates specifically tRNAAsp.Proc Natl Acad Sci U S A. 2004 May 18;101(20):7530-5. doi: 10.1073/pnas.0401634101. Epub 2004 Apr 19. Proc Natl Acad Sci U S A. 2004. PMID: 15096594 Free PMC article.
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A truncated aminoacyl-tRNA synthetase modifies RNA.Proc Natl Acad Sci U S A. 2004 May 18;101(20):7536-41. doi: 10.1073/pnas.0401982101. Epub 2004 Apr 19. Proc Natl Acad Sci U S A. 2004. PMID: 15096612 Free PMC article.
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