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Nucleic Acids Research, 2002, Vol. 30, No. 19 4186-4198
© 2002 Oxford University Press

Temperature-sensitive mutants of the exosome subunit Rrp43p show a deficiency in mRNA degradation and no longer interact with the exosome

Carla C. Oliveira*, Fernando A. Gonzales and Nilson I. T. Zanchin1

Department of Biochemistry, Chemistry Institute, USP, Av. Prof. Lineu Prestes 748, São Paulo, SP 05508-900, Brazil and 1 Center for Structural Molecular Biology, Synchrotron National Laboratory (LNLS), Campinas, SP, Brazil

*To whom correspondence should be addressed. Tel: +55 11 3091 3810; Fax: +55 11 3815 5579; Email: ccoliv{at}iq.usp.br

Rrp43p is a Saccharomyces cerevisiae exosome subunit involved in pre-rRNA processing which is found both in the nucleus and in the cytoplasm. So far, no function has been assigned to the cytoplasmic fraction of Rrp43p. We have addressed Rrp43p function by analyzing mRNA stability in three rrp43 temperature-sensitive (ts) strains, which carry different ts alleles (rrp43-1, rrp43-2 and rrp43-3), and by analyzing Rrp43p interactions with the remaining exosome subunits. In the ts strains, endogenous mRNAs (ACT1 and PAB1), as well as a heterologous reporter mRNA (CATpG) showed longer half-lives, relative to a control strain carrying wild-type RRP43. The mutants also accumulated a degradation intermediate of the reporter mRNA that is typical of defective mRNA decay. These results allow us to propose that Rrp43p is required for mRNA degradation. Rrp43p interacts with the exosome complex via Rrp46p, as determined by two-hybrid analyses. Interestingly, the rrp43 ts mutant proteins do not interact with Rrp46p, indicating that the ts phenotype may be caused by disruption of the Rrp43p– Rrp46p interaction. The ts strains also showed a pre-rRNA processing defect, which is consistent with previous studies on Rrp43p function.


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