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
相关论文
共 51 条
  • [1] A CONTINUOUS SPECTROPHOTOMETRIC ASSAY FOR THE ACTIVATION OF PLANT NAD KINASE BY CALMODULIN, CALCIUM(II), AND EUROPIUM(III) IONS
    AMANN, BT
    MULQUEEN, P
    HORROCKS, WD
    [J]. JOURNAL OF BIOCHEMICAL AND BIOPHYSICAL METHODS, 1992, 25 (04): : 207 - 217
  • [2] Comparison in Accumulation of Lanthanide Elements Among Three Brassicaceae Plant Sprouts
    Anan, Yasumi
    Awaya, Yumi
    Ogihara, Yurie
    Yoshida, Miyuki
    Yawata, Ayako
    Ogra, Yasumitsu
    [J]. BULLETIN OF ENVIRONMENTAL CONTAMINATION AND TOXICOLOGY, 2012, 89 (01) : 133 - 137
  • [3] De Novo Design of Ln(III) Coiled Coils for Imaging Applications
    Berwick, Matthew R.
    Lewis, David J.
    Jones, Andrew W.
    Parslow, Rosemary A.
    Dafforn, Timothy R.
    Cooper, Helen J.
    Wilkie, John
    Pikramenou, Zoe
    Britton, Melanie M.
    Peacock, Anna F. A.
    [J]. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 2014, 136 (04) : 1166 - 1169
  • [4] Luminescence resonance energy transfer between genetically encoded donor and acceptor for protein-protein interaction studies in the molecular chaperone HSP70/HSP90 complexes
    Bhattacharya, Kaushik
    Bernasconi, Lilia
    Picard, Didier
    [J]. SCIENTIFIC REPORTS, 2018, 8
  • [5] TERBIUM(III) EMISSION AS A PROBE OF CALCIUM(II) BINDING-SITES IN PROTEINS
    BRITTAIN, HG
    RICHARDSON, FS
    MARTIN, RB
    [J]. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 1976, 98 (25) : 8255 - 8260
  • [6] BURDA K, 1995, Z NATURFORSCH C, V50, P220, DOI 10.1515/znc-1995-3-410
  • [7] TOP-IDP-scale: A new amino acid scale measuring propensity for intrinsic disorder
    Campen, Andrew
    Williams, Ryan M.
    Brown, Celeste J.
    Meng, Jingwei
    Uversky, Vladimir N.
    Dunker, A. Keith
    [J]. PROTEIN AND PEPTIDE LETTERS, 2008, 15 (09) : 956 - 963
  • [8] Gadolinium-binding helix-turn-helix peptides: DNA-dependent MRI contrast agents
    Caravan, P
    Greenwood, JM
    Welch, JT
    Franklin, SJ
    [J]. CHEMICAL COMMUNICATIONS, 2003, (20) : 2574 - 2575
  • [9] Single-Chain Lanthanide Luminescence Biosensors for Cell-Based Imaging and Screening of Protein-Protein Interactions
    Chen, Ting
    Ha Pham
    Mohamadi, Ali
    Miller, Lawrence W.
    [J]. ISCIENCE, 2020, 23 (09)
  • [10] Effects of rare earth ions on activity of RuBPcase in tobacco
    Chen, WJ
    Gu, YH
    Zhao, GW
    Tao, Y
    Luo, JP
    Hu, TD
    [J]. PLANT SCIENCE, 2000, 152 (02) : 145 - 151