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Author Notes:

To whom correspondence should be addressed. Tel: +1 404 727 4546; Fax: +1 404 727 3452; Email: acorbe2@emory.edu

We gratefully acknowledge Allison Lange for her helpful discussions about site-directed mutagenesis and nuclear transport; Sara Leung for microscopy reagents, protocols and advice, and all other members of the Corbett and Fridovich-Keil laboratories for their many helpful discussions and contributions.

Conflict of interest statement. None declared.


Research Funding:

This work was supported in part by funds from the NSF (J.F.K.), funds from Nucleic Acids Research, 2007, Vol. 35, No. 20 6867 at Emory University Libraries on March 12, 2014 http://nar.oxfordjournals.org/ Downloaded from the Emory University Research Committee (J.F.K.), and a grant from the NIH (A.H.C.).

Funding to pay the Open Access publication charges for this article was waived by Oxford University Press.

Analysis of a predicted nuclear localization signal: implications for the intracellular localization and function of the Saccharomyces cerevisiae RNA-binding protein Scp160


Journal Title:

Nucleic Acids Research


Volume 35, Number 20


, Pages 6862-6869

Type of Work:

Article | Final Publisher PDF


Gene expression is controlled by RNA-binding proteins that modulate the synthesis, processing, transport and stability of various classes of RNA. Some RNA-binding proteins shuttle between the nucleus and cytoplasm and are thought to bind to RNA transcripts in the nucleus and remain bound during translocation to the cytoplasm. One RNA-binding protein that has been hypothesized to function in this manner is the Saccharomyces cerevisiae Scp160 protein. Although the steady-state localization of Scp160 is cytoplasmic, previous studies have identified putative nuclear localization (NLS) and nuclear export (NES) signals. The goal of this study was to test the hypothesis that Scp160 is a nucleocytoplasmic shuttling protein. We exploited a variety of yeast export mutants to capture any potential nuclear accumulation of Scp160 and found no evidence that Scp160 enters the nucleus. These localization studies were complemented by a mutational analysis of the predicted NLS. Results indicate that key basic residues within the predicted NLS of Scp160 can be altered without severely affecting Scp160 function. This finding has important implications for understanding the function of Scp160, which is likely limited to the cytoplasm. Additionally, our results provide strong evidence that the presence of a predicted nuclear localization signal within the sequence of a protein should not lead to the assumption that the protein enters the nucleus in the absence of additional experimental evidence.

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© 2007 The Author(s)

This is an Open Access work distributed under the terms of the Creative Commons Attribution-NonCommercial 2.0 Generic License (http://creativecommons.org/licenses/by-nc/2.0/).

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