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A chaperone for the 'guardian of the genome'
Date:9/7/2011

ed p53 variants in tumors are less stable than intact p53 and require Hsp90 all the more," explains Franz Hagn, corresponding author of the study. "When this interaction is inhibited, especially mutated p53 is disposed of. This allows the intact p53 to fulfill its function, eliminate damaged cells and prevent the cancer."

In their study, Kessler, Buchner and their team determined that p53 binds to not only, as previously assumed, to the middle domain of Hsp90, but also with a high affinity to a site in the C terminal domain of the protein. Negatively charged amino acids at both binding sites of Hsp90 are responsible for the stability of this bond. "These sites are similar to DNA, whose phosphate backbone is also negatively charged," explains Kessler. "So Hsp90 imitates p53's actual partner. The complex of both proteins is held together in this way." p53 retains its original state, all the while, allowing it to continue binding to DNA.


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Contact: Dr. Markus Bernards
bernards@zv.tum.de
0049-892-892-2562
Technische Universitaet Muenchen
Source:Eurekalert

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