Latent and active p53 are identical in conformation

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p53 is a nuclear phosphoprotein that regulates cellular fate after genotoxic stress through its role as a transcriptional regulator of genes involved in cell cycle control and apoptosis. The C-terminal region of p53 is known to negatively regulate sequence specific DNA-binding of p53; modifications to the C-terminus relieve this inhibition. Two models have been proposed to explain this latency: (i) an allosteric model in which the C-terminal domain interacts with another domain of p53 or (ii) a competitive model in which the C-terminal and the core domains compete for DNA binding. We have characterized latent and active forms of dimeric p53 using gel mobility shift assays and NMR spectroscopy. We show on the basis of chemical shifts that dimeric p53 both containing and lacking the C-terminal domain are identical in conformation and that the C-terminus does not interact with other p53 domains. Similarly, NMR spectra of isolated core and tetramerization domains confirm a modular p53 architecture. The data presented here rule out an allosteric model for the regulation of p53.
Publisher
NATURE AMERICA INC
Issue Date
2001-09
Language
English
Article Type
Article
Keywords

DNA-BINDING DOMAIN; OLIGOMERIZATION DOMAIN; MULTIDIMENSIONAL NMR; CHEMICAL-SHIFTS; PROTEIN; SITE; N-15; SPECTROSCOPY; MOLECULE; C-13

Citation

NATURE STRUCTURAL BIOLOGY, v.8, no.9, pp.756 - 760

ISSN
1072-8368
DOI
10.1038/nsb0901-756
URI
http://hdl.handle.net/10203/81368
Appears in Collection
BiS-Journal Papers(저널논문)
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