Riboswitch effectors as protein enzyme cofactors

  1. Jesse C. Cochrane1,3 and
  2. Scott A. Strobel1,2
  1. 1Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut 06520, USA
  2. 2Department of Chemistry, Yale University, New Haven, Connecticut 06520, USA

Abstract

The recently identified glmS ribozyme revealed that RNA enzymes, like protein enzymes, are capable of using small molecules as catalytic cofactors to promote chemical reactions. Flavin mononucleotide (FMN), S-adenosyl methionine (SAM), adenosyl cobalamin (AdoCbl), and thiamine pyrophosphate (TPP) are known ligands for RNA riboswitches in the control of gene expression, but are also catalytically powerful and ubiquitous cofactors in protein enzymes. If RNA, instead of just binding these molecules, could harness the chemical potential of the cofactor, it would significantly expand the enzymatic repertoire of ribozymes. Here we review the chemistry of AdoCbl, SAM, FMN, and TPP in protein enzymology and speculate on how these cofactors might have been used by ribozymes in the prebiotic RNA World or may still find application in modern biology.

Keywords

Footnotes

  • ↵3 Present address: Department of Molecular Biology, Massachusetts General Hospital, and Department of Genetics, Harvard Medical School, 185 Cambridge Street, Boston, MA 02114, USA.

  • Reprint requests to: Scott A. Strobel, Department of Molecular Biophysics and Biochemistry, Yale University, 260 Whitney Avenue, New Haven, CT 06520, USA; e-mail: scott.strobel{at}yale.edu; fax: (203) 432-5767.

  • Article published online ahead of print. Article and publication date are at http://www.rnajournal.org/cgi/doi/10.1261/rna.908408.

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  1. Published in Advance April 22, 2008, doi: 10.1261/rna.908408 RNA 14: 993-1002 Copyright © 2008 RNA Society

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