Abstract / Description of output
We have cloned and expressed the putative Caenorhabditis elegans orthologue for small glutamine-rich tetratricopeptide repeat-containing protein, now assigned the gene name sgt-1 in the C. elegans genome database. Characterization of the purified protein by cross-linking, mass spectrometry and gel filtration experiments provides unambiguous evidence that SGT-1 forms homo-dimers in solution. The hydrodynamic dimensions of SGT-1 dimers in relation to their molecular weight suggest a protein with a low level of compactness and an extended conformation. Human SGT has been shown to interact with and regulate the activity of heat shock proteins Hsp70 and Hsp90 via a TPR domain mediated interaction. The SGT TPR domain (SGT-1-TPR, residues 100-226) was cloned, purified and shown by ITC and CD analysis to interact with the C-terminal peptides of Hsp70 and Hsp90 with comparable affinities although there is no evidence of a recently proposed coupled binding-folding mechanism for TPR domains.
Original language | English |
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Pages (from-to) | 496-503 |
Number of pages | 8 |
Journal | BBA - Proteins and Proteomics |
Volume | 1784 |
Issue number | 3 |
DOIs | |
Publication status | Published - Mar 2008 |
Keywords / Materials (for Non-textual outputs)
- Small glutamine-rich tetratricopeptide repeat-containing protein
- SGT
- TPR
- Hsp70
- Hsp90
- Co-chaperone