E3 Ubiquitin Ligase SPL2 Is a Lanthanide-Binding Protein

被引:5
|
作者
Tracz, Michal [1 ]
Gorniak, Ireneusz [1 ,2 ]
Szczepaniak, Andrzej [1 ]
Bialek, Wojciech [1 ]
机构
[1] Univ Wroclaw, Dept Biophys, Fac Biotechnol, Joliot Curie 14a, PL-50383 Wroclaw, Poland
[2] Univ Virginia, Sch Med, Dept Mol Physiol & Biol Phys, Charlottesville, VA 22908 USA
关键词
ubiquitination; chloroplast; lanthanides; SPL2; CALCIUM-BINDING; AFFINITY; IONS; ACTIVATION; TRYPTOPHAN; DESIGN; PROBES; SITES; TOOLS; CIAP2;
D O I
10.3390/ijms22115712
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The SPL2 protein is an E3 ubiquitin ligase of unknown function. It is one of only three types of E3 ligases found in the outer membrane of plant chloroplasts. In this study, we show that the cytosolic fragment of SPL2 binds lanthanide ions, as evidenced by fluorescence measurements and circular dichroism spectroscopy. We also report that SPL2 undergoes conformational changes upon binding of both Ca2+ and La3+, as evidenced by its partial unfolding. However, these structural rearrangements do not interfere with SPL2 enzymatic activity, as the protein retains its ability to auto-ubiquitinate in vitro. The possible applications of lanthanide-based probes to identify protein interactions in vivo are also discussed. Taken together, the results of this study reveal that the SPL2 protein contains a lanthanide-binding site, showing for the first time that at least some E3 ubiquitin ligases are also capable of binding lanthanide ions.
引用
收藏
页数:19
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