Format

Send to

Choose Destination
EMBO J. 2001 Jan 15;20(1-2):118-27.

Identification of a structural motif that confers specific interaction with the WD40 repeat domain of Arabidopsis COP1.

Author information

1
Department of Molecular, Cellular and Developmental Biology, Yale University, OML 354, Yale University, PO Box 20-8104, 165 Prospect Street, New Haven, CT 06520-8104, USA.

Abstract

Arabidopsis COP1 is a photomorphogenesis repressor capable of directly interacting with the photomorphogenesis-promoting factor HY5. This interaction between HY5 and COP1 results in targeted deg radation of HY5 by the 26S proteasome. Here we characterized the WD40 repeat domain-mediated interactions of COP1 with HY5 and two new proteins. Mutational analysis of those interactive partners revealed a conserved motif responsible for the interaction with the WD40 domain. This novel motif, with the core sequence V-P-E/D-φ-G (φ = hydrophobic residue) in conjunction with an upstream stretch of 4-5 negatively charged residues, interacts with a defined surface area of the ss-propeller assembly of the COP1 WD40 repeat domain through both hydrophobic and ionic interactions. Several residues in the COP1 WD40 domain that are critical for the interaction with this motif have been revealed. The fact that point mutations either in the COP1 WD40 domain or in the HY5 motif that abolish the interaction between COP1 and HY5 in yeast result in a dramatic reduction of HY5 degradation in transgenic plants validates the biological significance of this defined interaction.

PMID:
11226162
PMCID:
PMC140188
DOI:
10.1093/emboj/20.1.118
[Indexed for MEDLINE]
Free PMC Article

Supplemental Content

Full text links

Icon for HighWire Icon for PubMed Central
Loading ...
Support Center