The cochaperone murine stress-inducible protein 1: overexpression, purification, and characterization

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van der Spuy, Jacqueline, Cheetham, Michael E, Dirr, Heini W and Blatch, Gregory L (2001) The cochaperone murine stress-inducible protein 1: overexpression, purification, and characterization. Protein Expression and Purification, 21 (3). pp. 462-469. ISSN 1046-5928

Abstract

Murine stress-inducible protein 1 (mSTI1) is a cochaperone that is homologous with the human heat shock cognate protein 70 (Hsc70)/heat shock protein 90 (Hsp90)-organizing protein (Hop). To analyze the biochemical properties of mSTI1 and the stoichiometry of the Hsc70.mSTI1.Hsp90 association, recombinant mSTI1 was produced in untagged, histidine (His)-tagged, and glutathione S-transferase (GST)-tagged forms. His-mSTI1 was detected either as a dimer during size-exclusion-high-performance liquid chromatography (SE-HPLC) or as a monomer during Superdex 200 gel filtration chromatography. SE-HPLC on GST-mSTI1 and untagged mSTI1 suggested that mSTI1 existed as a monomer. Cross-linking of His-mSTI1 detected a compact monomeric species and a dimeric species. Gel filtration on the association of bovine STI1 or His-mSTI1 with Hsc70 detected species of molecular mass consistent with a dimeric STI1 species or a 1:1 complex of STI1 and Hsc70. Our data and that of others suggest that mSTI1 and its homologues exist as either a monomer or a dimer and that this facilitates its proposed function as an Hsc70/Hsp90 organizing protein.

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Additional Information

Online ISSN: 1096-0279

Item type Article
URI https://vuir.vu.edu.au/id/eprint/8174
DOI https://doi.org/10.1006/prep.2001.1399
Official URL http://dx.doi.org/10.1006/prep.2001.1399
Subjects Historical > Faculty/School/Research Centre/Department > School of Biomedical and Health Sciences
Historical > FOR Classification > 0601 Biochemistry and Cell Biology
Keywords ResPubID22229. Hsc70, Hsp90, mSTI1, Hop, protein interaction, tetratricopeptide repeat motifs
Citations in Scopus 13 - View on Scopus
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