This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Keegan, L. P.
Right arrow Articles by O'Connell, M. A.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Keegan, L. P.
Right arrow Articles by O'Connell, M. A.

 Previous Article  |  Next Article 

Molecular and Cellular Biology, February 2000, p. 825-833, Vol. 20, No. 3
0270-7306/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

The Properties of a tRNA-Specific Adenosine Deaminase from Drosophila melanogaster Support an Evolutionary Link between Pre-mRNA Editing and tRNA Modification

Liam P. Keegan,1 André P. Gerber,2 Jim Brindle,1 Ronny Leemans,3 Angela Gallo,1 Walter Keller,2 and Mary A. O'Connell1,*

MRC Human Genetics Unit, Western General Hospital, Edinburgh EH4 2XU, United Kingdom,1 and Department of Cell Biology, Biozentrum of the University of Basel, CH-4056 Basel,2 and Zoological Institute, University of Basel, CH-4051 Basel,3 Switzerland

Received 16 August 1999/Returned for modification 30 September 1999/Accepted 1 November 1999

Pre-mRNA editing involving the conversion of adenosine to inosine is mediated by adenosine deaminases that act on RNA (ADAR1 and ADAR2). ADARs contain multiple double-stranded RNA(dsRNA)-binding domains in addition to an adenosine deaminase domain. An adenosine deaminase acting on tRNAs, scTad1p (also known as scADAT1), cloned from Saccharomyces cerevisiae has a deaminase domain related to the ADARs but lacks dsRNA-binding domains. We have identified a gene homologous to scADAT1 in the region of Drosophila melanogaster Adh chromosome II. Recombinant Drosophila ADAT1 (dADAT1) has been expressed in the yeast Pichia pastoris and purified. The enzyme has no activity on dsRNA substrates but is a tRNA deaminase with specificity for adenosine 37 of insect alanine tRNA. dADAT1 shows greater similarity to vertebrate ADARs than to yeast Tad1p, supporting the hypothesis of a common evolutionary origin for ADARs and ADATs. dAdat1 transcripts are maternally supplied in the egg. Zygotic expression is widespread initially and later concentrates in the central nervous system.

* Corresponding author. Mailing address: MRC Human Genetics Unit, Western General Hospital, Crewe Road, Edinburgh EH4 2XU, United Kingdom. Phone: 44-131-467 8417. Fax: 44-131-343 2620. E-mail: Mary.O'Connell{at}hgu.mrc.ac.uk.

Molecular and Cellular Biology, February 2000, p. 825-833, Vol. 20, No. 3
0270-7306/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:

  • Marcucci, R., Romano, M., Feiguin, F., O'Connell, M. A., Baralle, F. E. (2009). Dissecting the splicing mechanism of the Drosophila editing enzyme; dADAR. Nucleic Acids Res 37: 1663-1671 [Abstract] [Full Text]  
  • Mehler, M. F., Mattick, J. S. (2007). Noncoding RNAs and RNA Editing in Brain Development, Functional Diversification, and Neurological Disease. Physiol. Rev. 87: 799-823 [Abstract] [Full Text]  
  • Desterro, J. M. P., Keegan, L. P., Lafarga, M., Berciano, M. T., O'Connell, M., Carmo-Fonseca, M. (2003). Dynamic association of RNA-editing enzymes with the nucleolus. J. Cell Sci. 116: 1805-1818 [Abstract] [Full Text]  
  • Anantharaman, V., Koonin, E. V., Aravind, L. (2002). Comparative genomics and evolution of proteins involved in RNA metabolism. Nucleic Acids Res 30: 1427-1464 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»