Mapping a nucleolar targeting sequence of an RNA binding nucleolar protein, Nop25

Experimental Cell Research
Takashi FujiwaraJunya Tanaka

Abstract

Nop25 is a putative RNA binding nucleolar protein associated with rRNA transcription. The present study was undertaken to determine the mechanism of Nop25 localization in the nucleolus. Deletion experiments of Nop25 amino acid sequence showed Nop25 to contain a nuclear targeting sequence in the N-terminal and a nucleolar targeting sequence in the C-terminal. By expressing derivative peptides from the C-terminal as GFP-fusion proteins in the cells, a lysine and arginine residue-enriched peptide (KRKHPRRAQDSTKKPPSATRTSKTQRRRR) allowed a GFP-fusion protein to be transported and fully retained in the nucleolus. When the peptide was fused with cMyc epitope and expressed in the cells, a cMyc epitope was then detected in the nucleolus. Nop25 did not localize in the nucleolus by deletion of the peptide from Nop25. Furthermore, deletion of a subdomain (KRKHPRRAQ) in the peptide or amino acid substitution of lysine and arginine residues in the subdomain resulted in the loss of Nop25 nucleolar localization. These results suggest that the lysine and arginine residue-enriched peptide is the most prominent nucleolar targeting sequence of Nop25 and that the long stretch of basic residues might play an important role in the nucleolar localizat...Continue Reading

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Citations

May 26, 2007·Biochemical and Biophysical Research Communications·Shunji SuzukiMotoko Kanno
Jul 18, 2009·Cell Motility and the Cytoskeleton·Andrew J Lindsay, Mary W McCaffrey
Dec 17, 2009·Molecular Cell·Marlene OeffingerMichael P Rout
Oct 27, 2017·Nucleic Acids Research·Daniel D ScottMarlene Oeffinger
Aug 11, 2007·The EMBO Journal·Tom P MonieStephen Curry
Sep 22, 2020·The Journal of Biological Chemistry·Brendan W StevensonJessica K Holien
Jan 24, 2007·Experimental Cell Research·William S BrooksDavid F Crawford
Mar 19, 2015·ACS Applied Materials & Interfaces·Weimin LiuPengfei Wang

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