This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Supplemental material
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow E-mail this article to a friend
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 Nakai, Y.
Right arrow Articles by Hayashi, H.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Nakai, Y.
Right arrow Articles by Hayashi, H.

 Previous Article  |  Next Article 

Molecular and Cellular Biology, April 2007, p. 2841-2847, Vol. 27, No. 8
0270-7306/07/$08.00+0     doi:10.1128/MCB.01321-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

Thio Modification of Yeast Cytosolic tRNA Is an Iron-Sulfur Protein-Dependent Pathway{triangledown} ,{dagger}

Yumi Nakai,1* Masato Nakai,2 Roland Lill,3 Tsutomu Suzuki,4 and Hideyuki Hayashi1*

Department of Biochemistry, Osaka Medical College, 2-7 Daigakumachi, Takatsuki 569-8686, Japan,1 Institute for Protein Research, Osaka University, 3-2 Yamadaoka, Suita 565-0871, Japan,2 Institut für Zytobiologie und Zytopathologie, Philipps-Universität Marburg, Robert-Koch-Strasse 6, D-35033 Marburg, Germany,3 Department of Chemistry and Biotechnology, Graduate School of Engineering, University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-8656, Japan4

Received 18 July 2006/ Returned for modification 8 August 2006/ Accepted 22 January 2007

Defects in the yeast cysteine desulfurase Nfs1 cause a severe impairment in the 2-thio modification of uridine of mitochondrial tRNAs (mt-tRNAs) and cytosolic tRNAs (cy-tRNAs). Nfs1 can also provide the sulfur atoms of the iron-sulfur (Fe/S) clusters generated by the mitochondrial and cytosolic Fe/S cluster assembly machineries, termed ISC and CIA, respectively. Therefore, a key question remains as to whether the biosynthesis of Fe/S clusters is a prerequisite for the 2-thio modification of the tRNAs in both of the subcellular compartments of yeast cells. To elucidate this question, we asked whether mitochondrial ISC and/or cytosolic CIA components besides Nfs1 were involved in the 2-thio modification of these tRNAs. We demonstrate here that the three CIA components, Cfd1, Nbp35, and Cia1, are required for the 2-thio modification of cy-tRNAs but not of mt-tRNAs. Interestingly, the mitochondrial scaffold proteins Isu1 and Isu2 are required for the 2-thio modification of the cy-tRNAs but not of the mt-tRNAs, while mitochondrial Nfs1 is required for both 2-thio modifications. These results clearly indicate that the 2-thio modification of cy-tRNAs is Fe/S protein dependent and thus requires both CIA and ISC machineries but that of mt-tRNAs is Fe/S cluster independent and does not require key mitochondrial ISC components except for Nfs1.

* Corresponding author. Mailing address: Department of Biochemistry, Osaka Medical College, 2-7 Daigakumachi, Takatsuki 569-8686, Japan. Phone for Yumi Nakai: 81 726 83 1221, ext. 2453. Fax: 81 726 84 6516. E-mail: med004{at}art.osaka-med.ac.jp. E-mail: for Hideyuki Hayashi: hayashi{at}art.osaka-med.ac.jp

{triangledown} Published ahead of print on 5 February 2007.

{dagger} Supplemental material for this article may be found at http://mcb.asm.org/.

Molecular and Cellular Biology, April 2007, p. 2841-2847, Vol. 27, No. 8
0270-7306/07/$08.00+0     doi:10.1128/MCB.01321-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Bruske, E. I., Sendfeld, F., Schneider, A. (2009). Thiolated tRNAs of Trypanosoma brucei Are Imported into Mitochondria and Dethiolated after Import. J. Biol. Chem. 284: 36491-36499 [Abstract] [Full Text]  
  • Naamati, A., Regev-Rudzki, N., Galperin, S., Lill, R., Pines, O. (2009). Dual Targeting of Nfs1 and Discovery of Its Novel Processing Enzyme, Icp55. J. Biol. Chem. 284: 30200-30208 [Abstract] [Full Text]  
  • Noma, A., Sakaguchi, Y., Suzuki, T. (2009). Mechanistic characterization of the sulfur-relay system for eukaryotic 2-thiouridine biogenesis at tRNA wobble positions. Nucleic Acids Res 37: 1335-1352 [Abstract] [Full Text]  
  • Nakai, Y., Nakai, M., Hayashi, H. (2008). Thio-modification of Yeast Cytosolic tRNA Requires a Ubiquitin-related System That Resembles Bacterial Sulfur Transfer Systems. J. Biol. Chem. 283: 27469-27476 [Abstract] [Full Text]  
  • Huang, B., Lu, J., Bystrom, A. S. (2008). A genome-wide screen identifies genes required for formation of the wobble nucleoside 5-methoxycarbonylmethyl-2-thiouridine in Saccharomyces cerevisiae. RNA 14: 2183-2194 [Abstract] [Full Text]  
  • Marelja, Z., Stocklein, W., Nimtz, M., Leimkuhler, S. (2008). A Novel Role for Human Nfs1 in the Cytoplasm: Nfs1 ACTS AS A SULFUR DONOR FOR MOCS3, A PROTEIN INVOLVED IN MOLYBDENUM COFACTOR BIOSYNTHESIS. J. Biol. Chem. 283: 25178-25185 [Abstract] [Full Text]  


Copyright © 2010 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»