Poly(ADP-ribose) binds to specific domains of p53 and alters its DNA binding functions (Q28269174)

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J M Pleschke

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H E Kleczkowska

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F R Althaus

Journal of Biological Chemistry

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language of work or name

English

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publication date

8 May 1998

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published in

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volume

273

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issue

19

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page(s)

11839-43

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cites work

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Post-translational modification of poly(ADP-ribose) polymerase induced by DNA strand breaks

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Small peptides activate the latent sequence-specific DNA binding function of p53.

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Regulation of the specific DNA binding function of p53

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Identification of a region of p53 that confers lability

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Analysis of a protein-binding domain of p53

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ADP-ribosylation of p53 tumor suppressor protein: mutant but not wild-type p53 is modified

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ATM-dependent telomere loss in aging human diploid fibroblasts and DNA damage lead to the post-translational activation of p53 protein involving poly(ADP-ribose) polymerase.

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Wild-type but not mutant p53 immunopurified proteins bind to sequences adjacent to the SV40 origin of replication

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p53 binds single-stranded DNA ends and catalyzes DNA renaturation and strand transfer.

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Poly(ADP-ribose) quantification at the femtomole level in mammalian cells

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Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4

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Activation of p53 sequence-specific DNA bindingby short single strands of DNA requires the p53 C-terminus

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A transcriptionally active DNA-binding site for human p53 protein complexes

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Cooperative DNA binding of p53 with TFIID (TBP): a possible mechanism for transcriptional activation

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The p53 protein is an unusually shaped tetramer that binds directly to DNA.

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Regulation of the sequence-specific DNA binding function of p53 by protein kinase C and protein phosphatases

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p53 domains: identification and characterization of two autonomous DNA-binding regions.

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p53 binds single-stranded DNA ends through the C-terminal domain and internal DNA segments via the middle domain

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The single-stranded DNA end binding site of p53 coincides with the C-terminal regulatory region.

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Defective induction but normal activation and function of p53 in mouse cells lacking poly-ADP-ribose polymerase

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