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The m itochondrial protein t argeting s uppressor ( mts1 ) mutation maps to the mRNA‐binding domain of Npl3p and affects translation on cytoplasmic polysomes
Author(s) -
Gratzer Sabine,
Beilharz Traude,
Beddoe Travis,
Henry Michael F.,
Lithgow Trevor
Publication year - 2000
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1046/j.1365-2958.2000.01765.x
Subject(s) - polysome , biology , cytoplasm , translation (biology) , messenger rna , microbiology and biotechnology , rna binding protein , protein biosynthesis , rna , saccharomyces cerevisiae , mutant , biochemistry , ribosome , yeast , gene
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.