Please use this identifier to cite or link to this item: http://lib.jncasr.ac.in:8080/jspui/handle/10572/32
Title: The acidic C-terminal domain and A-box of HMGB-1 regulates p53-mediated transcription
Authors: Banerjee, Sourav
Kundu, Tapas K
Keywords: Mobility group protein-1
Activator-dependent transcription
Tata-binding protein
RNA-Polymerase-II
DNA-Binding
Chromosomal-proteins
P53
HMG-1
Acetylation
Identification
Issue Date: 15-Jun-2003
Publisher: Oxford University Press
Citation: Nucleic Acids Research 31(12), 3236-3247 (2003).
Abstract: p53 function is modulated by several covalent and non-covalent modifiers. The architectural DNA-binding protein, High Mobility Group protein B-1 is a unique activator of p53. HMGB-1 protein is structured into two HMG-box domains, namely A-box and B-box, connected to a long highly acidic C-terminal domain. Here we report that both the C-terminal domain and A-box of HMGB-1 are critical for stimulation of p53-mediated DNA binding to its cognate site. Though deletion of these domains showed minimal effect in activation of p53-mediated transcription from the DNA template as compared to full-length HMGB-1, truncation of both the domains indeed showed significant reduction of transcriptional activation from the chromatin template as observed in DNA binding. Using transient transfection assays we showed that the C-terminal acidic domain and A-box of HMGB-1 are critical for the enhancement of the p53-mediated transactivation in vivo. Furthermore, the C-terminal domain and A-box deleted HMGB-1 could not activate p53-dependent apoptosis above the basal level. In conclusion, these results elucidate the role of acidic C-terminal domain and A-box of HMGB-1 in p53-mediated transcriptional activation and its further downstream effect.
Description: Restricted access.
URI: http://hdl.handle.net/10572/32
Other Identifiers: 0305-1048
Appears in Collections:Research Papers (Tapas K. Kundu)

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