The TPR2B domain of the Hsp70/Hsp90 organizing protein (Hop) may contribute towards its dimerization.
The role of the TPR2B domain of Hop is as yet unknown. We have shown here by site directed mutagenesis and size exclusion chromatography for the first time that the TPR1 and TPR2B domains of Hop independently dimerized, and that the dimerization of TPR2B was not dependent on its predicted two-carboxylate clamp residues. Furthermore, our data indicated that the dimerization of Hop and its domains was not disrupted in the presence of Hsp70 and Hsp90 peptides.
Biomedical Biotechnology Research Unit, Department of Biochemistry, Microbiology and Biotechnology, Rhodes University, Grahamstown, South Africa. G.Blatch@ru.ac.za.
Victoria M
VM
Longshaw
Linda L
LL
Stephens
Sheril
S
Daniel
Gregory L
GL
Blatch
D000595:Amino Acid Sequence; D019281:Dimerization; D006360:Heat-Shock Proteins / Q000737:chemistry*; D008969:Molecular Sequence Data; D055503:Protein Multimerization; D017434:Protein Structure, Tertiary; D011506:Proteins / Q000302:isolation & purification; D016415:Sequence Alignment
D006360:Heat-Shock Proteins; D011506:Proteins; C079373:STIP1 protein, human