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Heterocomplex formation between metastasis‐related protein S100A4 (Mts1) and S100A1 as revealed by the yeast two‐hybrid system
Author(s) -
Tarabykina Svetlana,
Kriajevska Marina,
Scott David J.,
Hill Tessa J.,
Lafitte Daniel,
Derrick Peter J.,
Dodson Guy G.,
Lukanidin Eugene,
Bronstein Igor
Publication year - 2000
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(00)01652-5
Subject(s) - in vivo , electrospray ionization , yeast , chemistry , metastasis , mass spectrometry , saccharomyces cerevisiae , microbiology and biotechnology , biochemistry , biology , cancer research , biophysics , cancer , genetics , chromatography
S100A4 (Mts1) is a Ca 2+ ‐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 Cys 76 and/or Cys 81 of S100A4 by Ser abolishes the S100A4/S100A1 heterodimerization, but does not affect the S100A4 homodimerization in vivo.