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

Protein Expression and Purification

Volumn 21, Issue 3, 2001, Pages 462-469

  Van Der Spuy, Jacqueline ^a   Cheetham, Michael E ^b   Dirr, Heini W ^a   Blatch, Gregory L ^a  

^a UNIVERSITY OF THE WITWATERSRAND   (South Africa)

^b UNIVERSITY COLLEGE LONDON   (United Kingdom)

Author keywords

Hop; Hsc70; Hsp90; mSTI1; Protein protein interaction; Tetratricopeptide repeat motifs

Indexed keywords

BOVINAE; HUMULUS; MURINAE;

EID: 0035715002     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1006/prep.2001.1399     Document Type: Article

References (16)

1. Isolation of a mouse cDNA encoding mSTI1, a stress-inducible protein containing the TPR motif
2. Stress-inducible, murine protein mSTI1: Characterization of binding domains for heat shock proteins and in vitro phosphorylation by different kinases
3. Identification of a 60-kilodalton stress-related protein, p60, which interacts with hsp90 and hsp70
4. Interactions of p60, a mediator of progesterone receptor assembly, with heat shock proteins hsp90 and hsp70
5. Heat shock cognate protein 70 chaperone-binding site in the co-chaperone murine stress-inducible protein 1 maps to within three consecutive tetratricopeptide repeat motifs
6. The carboxy-terminal domain of Hsc70 provides binding sites for a distinct set of chaperone cofactors
7. Regulation of Hsp90 ATPase activity by tetratricopeptide repeat (TPR)-domain co-chaperones
8. Specific binding of tetratricopeptide repeat proteins to the C-terminal 12-kDa domain of hsp90
9. Protein expression using cotranslational fusion and cleavage of ubiquitin: Mutagenesis of the glutathione-binding site of human Pi class glutathione S-transferases
10. Self-association of the molecular chaperone HSC70
11. Polymerization of 70-kDa heat shock protein by yeast DnaJ in ATP
12. Interconversion of three differentially modified and assembled forms of BiP
13. Effect of nucleotides, peptides, and unfolded proteins on the self-association of the molecular chaperone HSC70
14. The COOH-terminal peptide binding domain is essential for self-association of the molecular chaperone HSC70
15. Oligomerization of the 17-kDa peptide-binding domain of the molecular chaperone HSC70
16. Aggregation of hsp70 and hsc70 in vivo is distinct and temperature-dependent and their chaperone function is directly related to non-aggregated forms