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J Biol Chem, Vol. 274, Issue 38, 27231-27236, September 17, 1999
A Novel Motif Mediates the Targeting of the
Arabidopsis COP1 Protein to Subnuclear Foci
Minviluz G.
Stacey and
Albrecht G.
von Arnim
From the Department of Botany, The University of Tennessee,
Knoxville, Tennessee 37996-1100
The constitutive photomorphogenesis 1 (COP1)
protein of Arabidopsis thaliana accumulates in discrete
subnuclear foci. To better understand the role of subnuclear
architecture in COP1-mediated gene expression, we investigated the
structural motifs of COP1 that mediate its localization to subnuclear
foci using mutational analysis with green fluorescent protein as a
reporter. In a transient expression assay, a subnuclear localization
signal consisting of 58 residues between amino acids 120 and 177 of
COP1 was able to confer speckled localization onto the heterologous
nuclear NIa protein from tobacco etch virus. The subnuclear
localization signal overlaps two previously characterized motifs, a
cytoplasmic localization signal and a putative -helical coiled-coil
domain that has been implicated in COP1 dimerization. Moreover,
phenotypically lethal mutations in the carboxyl-terminal WD-40 repeats
inhibited localization to subnuclear foci, consistent with a functional role for the accumulation of COP1 at subnuclear sites.
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.

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Copyright © 1999 by the American Society for Biochemistry and Molecular Biology.
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