Weird fingers: functional analysis of WIP domain proteins

Ingo Appelhagen; Gunnar Huep; Gui-Hua Lu; Georg Strompen; Bernd Weisshaar; Martin Sagasser

doi:10.1016/j.febslet.2010.06.007

Weird fingers: functional analysis of WIP domain proteins

FEBS Lett. 2010 Jul 16;584(14):3116-22. doi: 10.1016/j.febslet.2010.06.007. Epub 2010 Jun 10.

Authors

Ingo Appelhagen¹, Gunnar Huep, Gui-Hua Lu, Georg Strompen, Bernd Weisshaar, Martin Sagasser

Affiliation

¹ Department of Biology, Chair of Genome Research, Bielefeld University, Bielefeld, Germany.

PMID: 20541552
DOI: 10.1016/j.febslet.2010.06.007

Abstract

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.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Amino Acid Motifs / genetics
Mutation
Nuclear Localization Signals / genetics
Nuclear Localization Signals / metabolism
Plants / genetics
Plants / metabolism
Protein Structure, Tertiary / genetics
Zinc Fingers / genetics*

Substances

Nuclear Localization Signals