Heterocomplex formation between metastasis‐related protein S100A4 (Mts1) and S100A1 as revealed by the yeast two‐hybrid system

FEBS Letters

Lukanidin, Eugene¹  Scott, David J.²  Tarabykina, Svetlana¹  Kriajevska, Marina¹  Lafitte, Daniel³  Hill, Tessa J.³  Dodson, Guy G.²  Bronstein, Igor²  Derrick, Peter J.³ 

[1] Department of Molecular Cancer Biology, Danish Cancer Society, Strandboulevarden 49, Copenhagen 2100, Denmark;York Structural Biology Centre, Department of Chemistry, University of York, York YO10 5DD, UK;Institute of Mass-Spectrometry, Department of Chemistry, University of Warwick, Coventry CV4 7AL, UK

关键词: S100 protein;    Mts1;    Two-hybrid system;    Heterodimer;    BD;    DNA-binding domain of GAL4;    AD;    transcriptional activation domain of GAL4;    PCR;    polymerase chain reaction;   

DOI  :  10.1016/S0014-5793(00)01652-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

S100A4 (Mts1) is a Ca²⁺-binding protein of the S100 family. This protein plays an important role in promoting tumor metastasis. In order to identify S100A4 interacting proteins, we have applied the yeast two-hybrid system as an in vivo approach. By screening a mouse mammary adenocarcinoma library, we have demonstrated that S100A4 forms a heterocomplex with S100A1, another member of the S100 family. The non-covalent heterodimerization was confirmed by fluorescence spectroscopy and electrospray ionization Fourier transform ion cyclotron resonance mass spectrometry. Mutational analysis revealed that replacement of Cys⁷⁶ and/or Cys⁸¹ of S100A4 by Ser abolishes the S100A4/S100A1 heterodimerization, but does not affect the S100A4 homodimerization in vivo.

【 授权许可】

Unknown