FEBS Letters
Volume 584, Issue 2 , Pages 265-271, 21 January 2010

Do all modifications benefit all tRNAs?

Edited by Manuel Santos

  • Eric M. Phizicky

      Affiliations

    • Department of Biochemistry and Biophysics, University of Rochester School of Medicine, Rochester, NY 14642, USA
    • Center for RNA Biology, University of Rochester School of Medicine, Rochester, NY 14642, USA
    • Corresponding Author InformationCorresponding authors. Address: The Ohio State Center for RNA Biology and The Ohio State University Biochemistry Program, The Ohio State University, Columbus, OH 43210, USA (J.D. Alfonzo).
    • ,
  • Juan D. Alfonzo

      Affiliations

    • Department of Microbiology, The Ohio State University, Columbus, OH 43210, USA
    • The Ohio State Center for RNA Biology and The Ohio State University Biochemistry Program, The Ohio State University, Columbus, OH 43210, USA
    • Corresponding Author InformationCorresponding authors. Address: The Ohio State Center for RNA Biology and The Ohio State University Biochemistry Program, The Ohio State University, Columbus, OH 43210, USA (J.D. Alfonzo).

Received 27 October 2009; received in revised form 12 November 2009; accepted 13 November 2009. published online 19 November 2009.

Abstract 

Despite the universality of tRNA modifications, some tRNAs lacking specific modifications are subject to degradation pathways, while other tRNAs lacking the same modifications are resistant. Here, we suggest a model in which some modifications have minor, possibly redundant, roles in specific tRNAs. This model is consistent with the low specificity of some modification enzymes. Limitations of this model include the limited assays and growth conditions on which these conclusions are based, as well as the high specificity exhibited by many modification enzymes with important roles in translation. The specificity of these enzymes is often enhanced by complex substrate recognition patterns and sub-cellular compartmentalization.

Keywords: tRNA, Modification, Degradation, Methylation, Thiolation, Editing

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PII: S0014-5793(09)00962-4

doi:10.1016/j.febslet.2009.11.049

FEBS Letters
Volume 584, Issue 2 , Pages 265-271, 21 January 2010

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