The role of yeast serine/arginine(SR)-type mRNA-binding protein Npl3p and the DEAD-box helicase Dbp5p during translation
Final Report Abstract
A major challenge in current molecular biology is to understand how sequential steps in gene expression are coupled. Recently, much attention has been focused on the linkage of transcription, processing and mRNA-export. Our recent data identified the DEAD-box helicase Dbp5p, involved in mRNA export and the iron-sulfur (Fe/S) cluster containing protein Rli1p from Saccharomyces cerevisiae as novel translation termination factors. Physical interaction of Dbp5p was detected witheRF1, but not with eRF3. In contrast to that, Rli1p interacts with both termination factors. Both new termination factors show strong genetic interactions with both eukaryotic release factors eRF1 and eRF3. Mutant strains of DBP5 and the downregulation of RLII lead to defects in the recognition of the stop codon, reflected in a high readthrough activity. Moreover, we have shown that in mutants of DBP5, eRF3 is not recruited to the termination complex, suggesting that the dissociation of Dbp5p allows eRF3 entry into the complex. In summary, in our work identified and characterized Dbp5p and Rli1p as two novel translation termination factors that together with eRF1 and eRF3 mediate translation termination in eukaryotes.
Publications
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Khoshnevis, S., Gross, T., Rotte, C., Baierlein, C., Ficner, R. and Krebber, H.
