The mitochondrial protein targeting suppressor (mts1) mutation maps to the mRNA-binding domain of Npl3p and affects translation on cytoplasmic polysomes.

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 Microbiol

journal_title

Molecular microbiology

authors

Gratzer S,Beilharz T,Beddoe T,Henry MF,Lithgow T

doi

10.1046/j.1365-2958.2000.01765.x

subject

Has Abstract

pub_date

2000-03-01 00:00:00

pages

1277-85

issue

6

eissn

0950-382X

issn

1365-2958

pii

mmi1765

journal_volume

35

pub_type

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