Abstract:
:In all eukaryotic organisms, messenger RNA (mRNA) is synthesized in the nucleus and then exported to the cytoplasm for translation. The export reaction requires the concerted action of a large number of protein components, including a set of shuttle proteins that can exit and re-enter the nucleus through the nuclear pore complex. Here, we show that, in Saccharomyces cerevisiae, the shuttle protein Npl3p leaves the nuclear pore complex entirely and continues to function in the cytoplasm. A mutation at position 219 in its RNA-binding domain leaves Npl3p lingering in the cytoplasm associated with polysomes. Yeast cells expressing the mutant Npl3(L-219S) protein show alterations in mRNA stability that can affect protein synthesis. As a result, defects in nascent polypeptide targeting to subcellular compartments such as the mitochondria are also suppressed.
journal_name
Mol Microbioljournal_title
Molecular microbiologyauthors
Gratzer S,Beilharz T,Beddoe T,Henry MF,Lithgow Tdoi
10.1046/j.1365-2958.2000.01765.xsubject
Has Abstractpub_date
2000-03-01 00:00:00pages
1277-85issue
6eissn
0950-382Xissn
1365-2958pii
mmi1765journal_volume
35pub_type
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