GAL11P: A yeast mutation that potentiates the effect of weak GAL4-derived activators Export

@article{citeulike:3158589, abstract = {A mutant yeast in which a weak GAL4-derived activator functions as a strong activator bears a single missense mutation in GAL11 (a.k.a. SPT13). The first 74 amino acids of GAL4, including the zinc-dependent DNA binding region, attached to an acidic activating sequence, are sufficient to respond both to GAL11 and to our mutant GAL11P (potentiator). PPR1, a yeast activator with a similar zinc finger sequence, also responds to GAL11 and to GAL11P, whereas regulators bearing unrelated DNA binding motifs do not. GAL11 itself works as a strong activator when tethered to DNA by fusion to the bacterial LexA protein, and deletion of GAL11 is known to cause a 5- to 10-fold reduction in GAL4 activity. We suggest that a complex of GAL4 and GAL11 constitutes a particularly strong activator; evidence that the putative GAL4-GAL11 complex ordinarily forms preferentially on DNA suggests a biological rationale for GAL11 action.}, author = {Himmelfarb, Howard J. and Pearlberg, Joseph and Last, Douglas H. and Ptashne, Mark}, citeulike-article-id = {3158589}, citeulike-linkout-0 = {http://dx.doi.org/10.1016/0092-8674(90)90425-E}, citeulike-linkout-1 = {http://www.sciencedirect.com/science/article/B6WSN-4C593X2-1T/2/133999319f50e843e91b2c11454c6f48}, day = {21}, doi = {10.1016/0092-8674(90)90425-E}, journal = {Cell}, keywords = {gal4, mapplab-classic, med15gal11, pdr}, month = {December}, number = {6}, pages = {1299--1309}, posted-at = {2008-08-27 17:04:27}, priority = {2}, title = {GAL11P: A yeast mutation that potentiates the effect of weak GAL4-derived activators}, url = {http://dx.doi.org/10.1016/0092-8674(90)90425-E}, volume = {63}, year = {1990} }

TY - JOUR ID - citeulike:3158589 L3 - citeulike-article-id:3158589 N2 - A mutant yeast in which a weak GAL4-derived activator functions as a strong activator bears a single missense mutation in GAL11 (a.k.a. SPT13). The first 74 amino acids of GAL4, including the zinc-dependent DNA binding region, attached to an acidic activating sequence, are sufficient to respond both to GAL11 and to our mutant GAL11P (potentiator). PPR1, a yeast activator with a similar zinc finger sequence, also responds to GAL11 and to GAL11P, whereas regulators bearing unrelated DNA binding motifs do not. GAL11 itself works as a strong activator when tethered to DNA by fusion to the bacterial LexA protein, and deletion of GAL11 is known to cause a 5- to 10-fold reduction in GAL4 activity. We suggest that a complex of GAL4 and GAL11 constitutes a particularly strong activator; evidence that the putative GAL4-GAL11 complex ordinarily forms preferentially on DNA suggests a biological rationale for GAL11 action. IS - 6 JF - Cell EP - 1309 TI - GAL11P: A yeast mutation that potentiates the effect of weak GAL4-derived activators VL - 63 SP - 1299 KW - gal4 KW - mapplab-classic KW - med15gal11 KW - pdr AU - Himmelfarb, Howard AU - Pearlberg, Joseph AU - Last, Douglas AU - Ptashne, Mark PY - 1990/12/21/ UR - http://dx.doi.org/10.1016/0092-8674(90)90425-E ER -