Our results show that the mutant unfolds slightly faster than the wild-type with both wild-type and mutant proteins losing most of their native secondary structure within the first 2 ns.
We compared the circular dichroism (CD) spectra of the wild-type and mutant proteins losing DNA binding activities.
Most mutant p53 proteins lose their ability to bind wild-type p53 responsive elements and to regulate the expression of p53 transcriptional targets, thus losing tumor suppressor activity.
AIP appears to function as a tumor suppressor gene: we have previously reported data showing that mutant AIP proteins lose the ability of wild-type (WT AIPP to decrease cell proliferation and are unable to bind protein partners [ Leontiou et al., 2008].
Ethylene biosynthesis appeared to be the most sensitive assay for AtEHD2 activity, and the mutant proteins which lost functionality in the other assays employed herein still retained some ability to inhibit ethylene biosynthesis.
Replacement with alanine of any one of four conserved residues within the C-terminal domain of FusB (F156, K184, Y187, and F208) abrogated the ability of the protein to confer resistance to fusidic acid; the purified mutant proteins also lost the ability to bind S. aureus EF-G in vitro.
Intriguingly, unlike the DNA binding deficient TWIST1 mutants, the ΔWR truncation mutant protein completely lost its ability to activate the IL8 promoter.
This mutation results in haploinsufficiency of RUNX1, as the mutant protein has lost its capacity to bind DNA and to transactivate the expression of the target genes [ 9].
As predicted, the removal of the CTR containing the AHA motif generated a mutant protein which lost the ability to transactivate in this system, while the CTR alone was capable of transactivating when fused to GAL4-BD.
Earlier experiments clearly indicate that iron is required for the proper growth and Lkt production in M. haemolytica, as pathogenic gonococcal mutants devoid of these proteins lose their virulence [ 63, 64].
