Structural Basis for Dimerization in DNA Recognition by Gal4 Export

@article{citeulike:3021151, abstract = {Summary Gal4 is a Zn2Cys6 binuclear cluster containing transcription factor that binds DNA as a homodimer and can activate transcription by interacting with the mutant Gal11P protein. Although structures have been reported of the Gal4 dimerization domain and the binuclear cluster domain bound to DNA as a dimer, the structure of the "complete" Gal4 dimer bound to DNA has not previously been described. Here we report the structure of a complete Gal4 dimer bound to DNA and additional biochemical studies to address the molecular basis for Gal4 dimerization in DNA binding. We find that Gal4 dimerization on DNA is mediated by an intertwined helical bundle that deviates significantly from the solution NMR structure of the free dimerization domain. Associated biochemical studies show that the dimerization domain of Gal4 is important for DNA binding and protein thermostability. We also map the interaction surface of the Gal4 dimerization domain with Gal11P.}, author = {Hong, Manqing and Fitzgerald, Mary X. and Harper, Sandy and Luo, Cheng and Speicher, David W. and Marmorstein, Ronen}, citeulike-article-id = {3021151}, citeulike-linkout-0 = {http://dx.doi.org/10.1016/j.str.2008.03.015}, citeulike-linkout-1 = {http://www.sciencedirect.com/science/article/B6VSR-4SXYKHR-7/1/8b7a904980c574e35a46fbeb63dc5f91}, day = {9}, doi = {10.1016/j.str.2008.03.015}, journal = {Structure}, keywords = {crystal-structure, gal41-100, structure}, month = {July}, number = {7}, pages = {1019--1026}, posted-at = {2008-07-19 18:51:35}, priority = {3}, title = {Structural Basis for Dimerization in DNA Recognition by Gal4}, url = {http://dx.doi.org/10.1016/j.str.2008.03.015}, volume = {16}, year = {2008} }

TY - JOUR ID - citeulike:3021151 L3 - citeulike-article-id:3021151 N2 - Summary Gal4 is a Zn2Cys6 binuclear cluster containing transcription factor that binds DNA as a homodimer and can activate transcription by interacting with the mutant Gal11P protein. Although structures have been reported of the Gal4 dimerization domain and the binuclear cluster domain bound to DNA as a dimer, the structure of the "complete" Gal4 dimer bound to DNA has not previously been described. Here we report the structure of a complete Gal4 dimer bound to DNA and additional biochemical studies to address the molecular basis for Gal4 dimerization in DNA binding. We find that Gal4 dimerization on DNA is mediated by an intertwined helical bundle that deviates significantly from the solution NMR structure of the free dimerization domain. Associated biochemical studies show that the dimerization domain of Gal4 is important for DNA binding and protein thermostability. We also map the interaction surface of the Gal4 dimerization domain with Gal11P. IS - 7 JF - Structure EP - 1026 TI - Structural Basis for Dimerization in DNA Recognition by Gal4 VL - 16 SP - 1019 KW - crystal-structure KW - gal41-100 KW - structure AU - Hong, Manqing AU - Fitzgerald, Mary AU - Harper, Sandy AU - Luo, Cheng AU - Speicher, David AU - Marmorstein, Ronen PY - 2008/07/09/ UR - http://dx.doi.org/10.1016/j.str.2008.03.015 ER -