Document Detail


Kap104p imports the PY-NLS-containing transcription factor Tfg2p into the nucleus.
MedLine Citation:
PMID:  19366694     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
A previous bioinformatics study identified a putative PY-NLS in the yeast transcription factor Tfg2p (Suel, K. E., Gu, H., and Chook, Y. M. (2008) PLoS Biol. 6, e137). In this study, we validate Tfg2p as a Kap104p substrate and examine the energetic organization of its PY-NLS. The Tfg2p PY-NLS can target a heterologous protein into the cell nucleus through interactions with Kap104p. Surprisingly, full-length Tfg2p is still localized to the nucleus of Kap104p temperature-sensitive cells and, similarly, Tfg2p with a mutated PY-NLS is nuclear in wild-type cells. Other Karyopherinbetas (Kapbetas) such as Kap108p and Kap120p also bind Tfg2p and may import it into the nucleus. More importantly, we demonstrate that Tfg2p is retained in the nucleus through DNA binding. Mutations of DNA binding residues relieve nuclear retention and unmask the role of Kap104p in Tfg2p nuclear import. More generally, steady-state localization of a nuclear protein is dictated by its nuclear import and export activities as well as its interactions in the nucleus and the cytoplasm.
Authors:
Katherine E Süel; Yuh Min Chook
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't     Date:  2009-04-13
Journal Detail:
Title:  The Journal of biological chemistry     Volume:  284     ISSN:  0021-9258     ISO Abbreviation:  J. Biol. Chem.     Publication Date:  2009 Jun 
Date Detail:
Created Date:  2009-06-01     Completed Date:  2009-07-13     Revised Date:  2010-09-27    
Medline Journal Info:
Nlm Unique ID:  2985121R     Medline TA:  J Biol Chem     Country:  United States    
Other Details:
Languages:  eng     Pagination:  15416-24     Citation Subset:  IM    
Affiliation:
Department of Pharmacology, University of Texas Southwestern Medical Center, Dallas, Texas 75390, USA.
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
Binding Sites
Cloning, Molecular
Escherichia coli / genetics
Glutathione Transferase / genetics
Karyopherins / metabolism*
Molecular Sequence Data
Peptide Fragments / genetics
Plasmids
Recombinant Fusion Proteins / metabolism
Restriction Mapping
Saccharomyces cerevisiae / genetics*,  metabolism
Saccharomyces cerevisiae Proteins / genetics,  metabolism*
Transcription Factors / genetics*
beta Karyopherins
Grant Support
ID/Acronym/Agency:
5-T32-GM008297/GM/NIGMS NIH HHS; R01-GM069909/GM/NIGMS NIH HHS
Chemical
Reg. No./Substance:
0/KAP104 protein, S cerevisiae; 0/Karyopherins; 0/Peptide Fragments; 0/Recombinant Fusion Proteins; 0/Saccharomyces cerevisiae Proteins; 0/Transcription Factors; 0/beta Karyopherins; EC 2.5.1.18/Glutathione Transferase
Comments/Corrections

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