Redox regulation of fos and jun DNA-binding activity in vitro. Export

@article{citeulike:3909665, abstract = {The proto-oncogenes c-fos and c-jun function cooperatively as inducible transcription factors in signal transduction processes. Their protein products, Fos and Jun, form a heterodimeric complex that interacts with the DNA regulatory element known as the activator protein-1 (AP-1) binding site. Dimerization occurs via interaction between leucine zipper domains and serves to bring into proper juxtaposition a region in each protein that is rich in basic amino acids and that forms a DNA-binding domain. DNA binding of the Fos-Jun heterodimer was modulated by reduction-oxidation (redox) of a single conserved cysteine residue in the DNA-binding domains of the two proteins. Furthermore, a nuclear protein was identified that reduced Fos and Jun and stimulated DNA-binding activity in vitro. These results suggest that transcriptional activity mediated by AP-1 binding factors may be regulated by a redox mechanism.}, author = {Abate, C. and Patel, L. and Rauscher, F. J. and Curran, T.}, citeulike-article-id = {3909665}, citeulike-linkout-0 = {http://view.ncbi.nlm.nih.gov/pubmed/2118682}, citeulike-linkout-1 = {http://www.hubmed.org/display.cgi?uids=2118682}, day = {7}, issn = {0036-8075}, journal = {Science (New York, N.Y.)}, keywords = {cysteine}, month = {September}, number = {4973}, pages = {1157--1161}, posted-at = {2009-06-10 20:07:25}, priority = {2}, title = {Redox regulation of fos and jun DNA-binding activity in vitro.}, url = {http://view.ncbi.nlm.nih.gov/pubmed/2118682}, volume = {249}, year = {1990} }

TY - JOUR ID - citeulike:3909665 L3 - citeulike-article-id:3909665 N2 - The proto-oncogenes c-fos and c-jun function cooperatively as inducible transcription factors in signal transduction processes. Their protein products, Fos and Jun, form a heterodimeric complex that interacts with the DNA regulatory element known as the activator protein-1 (AP-1) binding site. Dimerization occurs via interaction between leucine zipper domains and serves to bring into proper juxtaposition a region in each protein that is rich in basic amino acids and that forms a DNA-binding domain. DNA binding of the Fos-Jun heterodimer was modulated by reduction-oxidation (redox) of a single conserved cysteine residue in the DNA-binding domains of the two proteins. Furthermore, a nuclear protein was identified that reduced Fos and Jun and stimulated DNA-binding activity in vitro. These results suggest that transcriptional activity mediated by AP-1 binding factors may be regulated by a redox mechanism. IS - 4973 JF - Science (New York, N.Y.) SN - 0036-8075 EP - 1161 TI - Redox regulation of fos and jun DNA-binding activity in vitro. VL - 249 SP - 1157 KW - cysteine AU - Abate, C AU - Patel, L AU - Rauscher, FJ AU - Curran, T PY - 1990/09/07/ UR - http://view.ncbi.nlm.nih.gov/pubmed/2118682 ER -