ASSOCIATION OF MYN, THE MURINE HOMOLOG OF MAX, WITH C-MYC STIMULATES METHYLATION-SENSITIVE DNA-BINDING AND RAS COTRANSFORMATION
ASSOCIATION OF MYN, THE MURINE HOMOLOG OF MAX, WITH C-MYC STIMULATES METHYLATION-SENSITIVE DNA-BINDING AND RAS COTRANSFORMATION
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DOI：
10.1016/0092-8674(91)90457-a
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发表时间：
1991-05-03
期刊：
影响因子：
64.5
通讯作者：
ZIFF, EB
中科院分区：
文献类型：
--
作者：
PRENDERGAST, GC;LAWE, D;ZIFF, EB
Myn是一种新的约18kd的小鼠碱性/螺旋-环-螺旋/“亮氨酸拉链”（B/HLH/LZ）蛋白，通过两种蛋白中的HLH/LZ基序与c-Myc癌蛋白形成特异性的dna结合复合物。c-Myc/Myn识别c-Myc结合位点（GACCACGTGGTC），其亲和力高于任何一种蛋白本身。识别位点的CpG甲基化极大地抑制了DNA结合，提示DNA甲基化可能在体内调节c-Myc/Myn复合物。在3T3成纤维细胞中，Myn mRNA水平被具有延迟早期动力学的血清诱导数倍，表明由即时早期基因产物调节。Myn在myc/ras大鼠胚胎成纤维细胞病灶形成实验中的共表达特异性增强了c-myc转化活性。我们认为Myn与c-Myc的相互作用稳定了体内序列特异性DNA结合。
Myn, a novel murine approximately 18 kd basic/helix-loop-helix/"leucine zipper" (B/HLH/LZ) protein, forms a specific DNA-binding complex with the c-Myc oncoprotein through the HLH/LZ motif in both proteins. c-Myc/Myn recognizes a c-Myc-binding site (GACCACGTGGTC) with higher affinity than either protein by itself. CpG methylation of the recognition site greatly inhibits DNA binding, suggesting that DNA methylation may regulate the c-Myc/Myn complex in vivo. In 3T3 fibroblasts, Myn mRNA levels are induced several-fold by serum with delayed early kinetics, suggesting regulation by immediate-early gene products. Coexpression of Myn in a myc/ras rat embryo fibroblast focus formation assay specifically augmented c-myc transforming activity. We suggest that interaction of Myn with c-Myc stabilizes sequence-specific DNA binding in vivo.