Weird fingers: functional analysis of WIP domain proteins.
WIP proteins form a plant specific subfamily of C2H2 zinc finger (ZF) proteins. In this study, we functionally characterized the WIP domain, which consists of four ZF motifs, and discuss molecular functions for WIP proteins. Mutations in each of the ZFs lead to loss of function of the TT1/WIP1 protein in Arabiopsis thaliana. SV40 type nuclear localisation signals were detected in two of the ZFs and functionally characterized using GFP fusions as well as new mutant alleles identified by TILLING. Promoter swap experiments showed that selected WIP proteins are partially able to take over TT1 function. Activity of the AtBAN promoter, a potential TT1 target, could be increased by the addition of TT1 to the TT2-TT8-TTG1 regulatory complex.
Appelhagen
Ingo
I
Department of Biology, Chair of Genome Research, Bielefeld University, Bielefeld, Germany.
Huep
Gunnar
G
Lu
Gui-Hua
GH
Strompen
Georg
G
Weisshaar
Bernd
B
Sagasser
Martin
M
D020816:Amino Acid Motifs / Q000235:genetics; D009154:Mutation; D019913:Nuclear Localization Signals / Q000235:genetics / Q000378:metabolism; D010944:Plants / Q000235:genetics / Q000378:metabolism; D017434:Protein Structure, Tertiary / Q000235:genetics; D016335:Zinc Fingers / Q000235:genetics*
D019913:Nuclear Localization Signals