This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Wang, S S Articles by Hopper, A K Search for Related Content PubMed PubMed Citation Articles by Wang, S S Articles by Hopper, A K

 Previous Article  |  Next Article 

Mol Cell Biol. 1988 December; 8(12): 5140-5149

Isolation of a yeast gene involved in species-specific pre-tRNA processing.

Department of Biological Chemistry, Milton S. Hershey Medical Center, Pennsylvania State University 17033.

ABSTRACT

To identify genes involved in pre-tRNA processing, we searched for yeast DNA sequences that specifically enhanced the expression of the SUP4(G37) gene. The SUP4(G37) gene possesses a point mutation at position 37 of suppressor tRNA(Tyr). This lesion results in a reduced rate of pre-tRNA splicing and a decreased level of nonsense suppression. A SUP4(G37) strain was transformed with a yeast genomic library, and the transformants were screened for increased suppressor activity. One transformant contained a plasmid that encoded an unessential gene, STP1, that in multiple copies enhanced the suppression of SUP4(G37) and caused increased production of mature SUP4(G37) product. Disruption of the genomic copy of STP1 resulted in a reduced efficiency of SUP4-mediated suppression and the accumulation of pre-tRNAs. Not all intron-containing pre-tRNAs were affected by the stp1-disruption. At least five of the nine families of pre-tRNAs were affected. Two other species, pre-tRNA(Ile) and pre-tRNA(3Leu), were not. We propose that STP1 encodes a tRNA species-specific product that functions as a helper for pre-tRNA splicing. The STP1 product may interact with pre-tRNAs to generate a structure that is efficiently recognized by splicing machinery.

This article has been cited by other articles:

• Whitney, M. L., Hurto, R. L., Shaheen, H. H., Hopper, A. K. (2007). Rapid and Reversible Nuclear Accumulation of Cytoplasmic tRNA in Response to Nutrient Availability. Mol. Biol. Cell 18: 2678-2686 [Abstract] [Full Text]  
• de Mayolo, A. A., Lisby, M., Erdeniz, N., Thybo, T., Mortensen, U. H., Rothstein, R. (2006). Multiple start codons and phosphorylation result in discrete Rad52 protein species.. Nucleic Acids Res 34: 2587-2597 [Abstract] [Full Text]  
• Stanford, D. R., Whitney, M. L., Hurto, R. L., Eisaman, D. M., Shen, W.-C., Hopper, A. K. (2004). Division of Labor Among the Yeast Sol Proteins Implicated in tRNA Nuclear Export and Carbohydrate Metabolism. Genetics 168: 117-127 [Abstract] [Full Text]  
• Forsberg, H., Ljungdahl, P. O. (2001). Genetic and Biochemical Analysis of the Yeast Plasma Membrane Ssy1p-Ptr3p-Ssy5p Sensor of Extracellular Amino Acids. Mol. Cell. Biol. 21: 814-826 [Abstract] [Full Text]  
• Boer, M. d., Nielsen, P. S., Bebelman, J.-P., Heerikhuizen, H. v., Andersen, H. A., Planta, R. J. (2000). Stp1p, Stp2p and Abf1p are involved in regulation of expression of the amino acid transporter gene BAP3 of Saccharomyces cerevisiae. Nucleic Acids Res 28: 974-981 [Abstract] [Full Text]  
• Sarkar, S., Azad, A. K., Hopper, A. K. (1999). Nuclear tRNA aminoacylation and its role in nuclear export of endogenous tRNAs in Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. USA 96: 14366-14371 [Abstract] [Full Text]  
• Sarkar, S., Hopper, A. K. (1998). tRNA Nuclear Export in Saccharomyces cerevisiae: In Situ Hybridization Analysis. Mol. Biol. Cell 9: 3041-3055 [Abstract] [Full Text]