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- W2117556297 endingPage "8653" @default.
- W2117556297 startingPage "8637" @default.
- W2117556297 abstract "Structural and biochemical studies have demonstrated that p73, p63 and p53 recognize DNA with identical amino acids and similar binding affinity. Here, measuring transactivation activity for a large number of response elements (REs) in yeast and human cell lines, we show that p53 family proteins also have overlapping transactivation profiles. We identified mutations at conserved amino acids of loops L1 and L3 in the DNA-binding domain that tune the transactivation potential nearly equally in p73, p63 and p53. For example, the mutant S139F in p73 has higher transactivation potential towards selected REs, enhanced DNA-binding cooperativity in vitro and a flexible loop L1 as seen in the crystal structure of the protein–DNA complex. By studying, how variations in the RE sequence affect transactivation specificity, we discovered a RE-transactivation code that predicts enhanced transactivation; this correlation is stronger for promoters of genes associated with apoptosis." @default.
- W2117556297 created "2016-06-24" @default.
- W2117556297 creator A5000170576 @default.
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- W2117556297 creator A5044744188 @default.
- W2117556297 creator A5050390217 @default.
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- W2117556297 creator A5066029953 @default.
- W2117556297 creator A5076007073 @default.
- W2117556297 creator A5086926095 @default.
- W2117556297 date "2013-07-26" @default.
- W2117556297 modified "2023-09-30" @default.
- W2117556297 title "Transactivation specificity is conserved among p53 family proteins and depends on a response element sequence code" @default.
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