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Identification of a portable repression domain and an E1A-responsive activation domain in Pax4: a possible role of Pax4 as a transcriptional repressor in the pancreas 总被引:4,自引:0,他引:4 下载免费PDF全文
Fujitani Y Kajimoto Y Yasuda T Matsuoka TA Kaneto H Umayahara Y Fujita N Watada H Miyazaki JI Yamasaki Y Hori M 《Molecular and cellular biology》1999,19(12):8281-8291
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Kozmik Z Daube M Frei E Norman B Kos L Dishaw LJ Noll M Piatigorsky J 《Developmental cell》2003,5(5):773-785
PaxB from Tripedalia cystophora, a cubomedusan jellyfish possessing complex eyes (ocelli), was characterized. PaxB, the only Pax gene found in this cnidarian, is expressed in the larva, retina, lens, and statocyst. PaxB contains a Pax2/5/8-type paired domain and octapeptide, but a Pax6 prd-type homeodomain. Pax2/5/8-like properties of PaxB include a DNA binding specificity of the paired domain, activation and inhibitory domains, and the ability to rescue spa(pol), a Drosophila Pax2 eye mutant. Like Pax6, PaxB activates jellyfish crystallin and Drosophila rhodopsin rh6 promoters and induces small ectopic eyes in Drosophila. Pax6 has been considered a "master" control gene for eye development. Our data suggest that the ancestor of jellyfish PaxB, a PaxB-like protein, was the primordial Pax protein in eye evolution and that Pax6-like genes evolved in triploblasts after separation from Cnidaria, raising the possibility that cnidarian and sophisticated triploblastic eyes arose independently. 相似文献
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Alvarez-Fernández M Halim VA Aprelia M Laoukili J Mohammed S Medema RH 《The Journal of biological chemistry》2011,286(38):33029-33036
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