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• W2010172919 endingPage "731" @default.
• W2010172919 startingPage "724" @default.
• W2010172919 abstract "A tryptophan-free Bacillus licheniformis nucleotide exchange factor (BlGrpE) and its Trp mutants (F70W, F103W, F149W, F70/103W, F70/149W, F103/149W and F70/103/149W) were over-expressed and purified to near homogeneity. Simultaneous addition of B. licheniformis DnaJ, NR-peptide and individual variants synergistically stimulated the ATPase activity of a recombinant DnaK (BlDnaK) from the same bacterium by 3.1–14.7-fold, which are significantly lower than the synergistic stimulation (18.9-fold) of BlGrpE. Protein–protein interaction analysis revealed that Trp mutants relevant to amino acid positions 103 and 149 lost the ability to bind BlDnaK. Circular dichroism measurements indicate that F70W displayed a comparable level of secondary structure to that of BlGrpE, and the wild-type protein and the Trp mutants as well all experienced a reversible behavior of thermal denaturation. Guanidine hydrochloride (GdnHCl)-induced unfolding transition for BlGrpE was calculated to be 1.25 M corresponding to ΔGN–U of 4.29 kcal/mol, whereas the unfolding transitions of mutant proteins were in the range of 0.77–1.31 M equivalent to ΔGN–U of 2.41–4.14 kcal/mol. Taken together, the introduction of tryptophan residue, especially at positions 103 and 149, into the primary structure of BlGrpE has been proven to be detrimental to structural integrity and proper function of the protein." @default.
• W2010172919 created "2016-06-24" @default.
• W2010172919 creator A5001851397 @default.
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• W2010172919 date "2015-01-01" @default.
• W2010172919 modified "2023-10-16" @default.
• W2010172919 title "Residues Phe103 and Phe149 are critical for the co-chaperone activity of Bacillus licheniformis GrpE" @default.
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• W2010172919 doi "https://doi.org/10.1016/j.ijbiomac.2014.09.013" @default.
• W2010172919 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/25246164" @default.
• W2010172919 hasPublicationYear "2015" @default.
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