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EMBO reports 4, 12, 1156–1162 (2003)
doi:10.1038/sj.embor.7400026
Published online: 7 November 2003
Formation and nuclear export of tRNA, rRNA and mRNA is regulated by the ubiquitin ligase Rsp5p
Silvia Neumann1, Elisabeth Petfalski2, Britta Brügger1, Helge Gro hans1, Felix Wieland1, David Tollervey2 & Ed Hurt1
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1 Biochemie-Zentrum Heidelberg (BZH),
Im Neuenheimer Feld 328, D-69120
Heidelberg, Germany
2 Wellcome Trust Centre for Cell Biology,
University of Edinburgh, Edinburgh EH9 3JR,
UK
To whom correspondence should be addressed
Ed Hurt Tel: +49 6221 544173; Fax: +49 6221 544369; E-mail:
cg5@ix.urz.uni-heidelberg.de
Received 29 July 2003; Accepted 22 September 2003; Published online 7 November 2003.
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Abstract
The yeast ubiquitin-protein ligase Rsp5p regulates processes as
diverse as polII transcription and endocytosis. Here, we identify Rsp5p in a
screen for tRNA export (tex) mutants. The tex23-1/rsp5-3
mutant, which is complemented by RSP5, not only shows a strong nuclear
accumulation of tRNAs at the restrictive temperature, but also is severely
impaired in the nuclear export of mRNAs and 60S pre-ribosomal subunits. In
contrast, nuclear localization sequence (NLS)-mediated nuclear protein import
is unaffected in this mutant. Strikingly, the nuclear RNA export defects seen
in the rsp5-3 strain are accompanied by a dramatic inhibition of both
rRNA and tRNA processing, a combination of phenotypes that has not been
reported for any previously characterized mutation in yeast. These data
implicate ubiquitination as a mechanism coordinating the major nuclear RNA
biogenesis pathways.
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