Format

Send to

Choose Destination
See comment in PubMed Commons below
Biochim Biophys Acta. 2008 Jun;1783(6):1200-10. doi: 10.1016/j.bbamcr.2008.01.031. Epub 2008 Feb 20.

The nuclear localization of Drosophila Hsp27 is dependent on a monopartite arginine-rich NLS and is uncoupled from its association to nuclear speckles.

Author information

1
Laboratory of Cellular and Developmental Genetics, Department of Medicine and CREFSIP, Université Laval, Québec, QC, Canada G1K 7P4.

Abstract

Drosophila Hsp27 is a small heat shock protein displaying exclusive nuclear localization both before and after heat shock. However, the mechanism implicated in this nuclear localization as well as the required sequences, are undefined. This study identifies the Hsp27 sequences mediating its nuclear localization. The generation of chimeric fusions between Hsp27 and Hsp23, a small heat shock protein displaying exclusive cytoplasmic localization, delineated a stretch of 15 amino acids containing a nuclear-targeting activity. Site-directed mutagenesis within this region unveiled the implication of three arginine residues (R54-R55-R56), which differentially combine to form a novel kind of nuclear localization signal (NLS). Abrogation of the nuclear localization signal activity indicated that Drosophila Hsp27 could still enter the nucleus to associate with nuclear speckles in a NLS-independent fashion. Mutagenesis of a putative nuclear export signal unveiled two leucine residues (L50 and L52) specifically involved in the association of Hsp27 to nuclear speckles and revealed novel nuclear structures formed by this Hsp27 mutant. The present study identifies two distinct sets of sequences respectively mediating the nuclear import of Hsp27 and its association to nuclear speckles. These two phenomena are uncoupled and can be separately abrogated.

PMID:
18339325
DOI:
10.1016/j.bbamcr.2008.01.031
[Indexed for MEDLINE]
Free full text
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for Elsevier Science
    Loading ...
    Support Center