Další formáty:
BibTeX
LaTeX
RIS
@article{1415822, author = {Štros, Michal and Kučírek, Martin and Abbasi Sani, Soodabeh and Polanská, Eva}, issn = {1874-9399}, journal = {Biochimica et Biophysica Acta}, title = {HMGB1-mediated DNA bending: Distinct roles in increasing p53 binding to DNA and the transactivation of p53-responsive gene promoters.}, url = {https://www.ncbi.nlm.nih.gov/pubmed/29421308}, year = {2018} }
TY - JOUR ID - 1415822 AU - Štros, Michal - Kučírek, Martin - Abbasi Sani, Soodabeh - Polanská, Eva PY - 2018 TI - HMGB1-mediated DNA bending: Distinct roles in increasing p53 binding to DNA and the transactivation of p53-responsive gene promoters. JF - Biochimica et Biophysica Acta SN - 18749399 UR - https://www.ncbi.nlm.nih.gov/pubmed/29421308 N2 - HMGB1 is a chromatin-associated protein that has been implicated in many important biological processes such as transcription, recombination, DNA repair, and genome stability. These functions include the enhancement of binding of a number of transcription factors, including the tumor suppressor protein p53, to their specific DNA-binding sites. HMGB1 is composed of two highly conserved HMG boxes, linked to an intrinsically disordered acidic C-terminal tail. Previous reports have suggested that the ability of HMGB1 to bend DNA may explain the in vitro HMGB1-mediated increase in sequence-specific DNA binding by p53. The aim of this study was to reinvestigate the importance of HMGB1-induced DNA bending in relationship to the ability of the protein to promote the specific binding of p53 to short DNA duplexes in vitro, and to transactivate two major p53-regulated human genes: Mdm2 and p21/WAF1. Using a number of HMGB1 mutants, we report that the HMGB1-mediated increase in sequence-specific p53 binding to DNA duplexes in vitro depends very little on HMGB1-mediated DNA bending. The presence of the acidic C-terminal tail of HMGB1 and/or the oxidation of the protein can reduce the HMGB1-mediated p53 binding. Interestingly, the induction of transactivation of p53-responsive gene promoters by HMGB1 requires both the ability of the protein to bend DNA and the acidic C-terminal tail, and is promoter-specific. We propose that the efficient transactivation of p53-responsive gene promoters by HMGB1 depends on complex events, rather than solely on the promotion of p53 binding to its DNA cognate sites. ER -
ŠTROS, Michal, Martin KUČÍREK, Soodabeh ABBASI SANI a Eva POLANSKÁ. HMGB1-mediated DNA bending: Distinct roles in increasing p53 binding to DNA and the transactivation of p53-responsive gene promoters. \textit{Biochimica et Biophysica Acta}. 2018. ISSN~1874-9399.
|