Researchers are exploring whether these ubiquitous fluorinated molecules might worsen infections or hamper vaccine effectiveness.
Image credit: Shutterstock/Dmitry Naumov.
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Edited by Harry F. Noller, University of California Santa Cruz, Santa Cruz, CA, and approved January 27, 2010 (received for review November 14, 2009)
Abstract
An indispensable step in protein biosynthesis is the 2′(3′) aminoacylation of tRNA by aminoacyl-tRNA synthetases. Here we show that a similar activity exists in a tiny, 5-nt-long RNA enzyme with a 3-nt active center. The small ribozyme initially trans-phenylalanylates a partially complementary 4-nt RNA selectively at its terminal 2′-ribose hydroxyl using PheAMP, the natural form for activated amino acid. The initial 2′ Phe-RNA product can be elaborated into multiple peptidyl-RNAs. Reactions do not require divalent cations, and have limited dependence on monovalent cations. Small size and minimal requirements for regiospecific translational activity strongly support the hypothesis that minuscule RNA enzymes participated in early forms of translation.
Footnotes
- 1To whom correspondence should be addressed. E-mail: yarus{at}stripe.colorado.edu.
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Author contributions: R.M.T. and M.Y. designed research; R.M.T. performed research; N.V.C. contributed new reagents/analytic tools; M.Y. analyzed data; and R.M.T. and M.Y. wrote the paper.
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The authors declare no conflict of interest.
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This article is a PNAS Direct Submission.
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This article contains supporting information online at www.pnas.org/cgi/content/full/0912895107/DCSupplemental.
Multiple translational products from a five-nucleotide ribozyme
Article Classifications
- Biological Sciences
- Biochemistry
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