ASSOCIATION OF MYN, THE MURINE HOMOLOG OF MAX, WITH C-MYC STIMULATES METHYLATION-SENSITIVE DNA-BINDING AND RAS COTRANSFORMATION

被引：566
作者：
PRENDERGAST, GC [1 ]
LAWE, D [1 ]
ZIFF, EB [1 ]
机构：
[1] NYU MED CTR,DEPT BIOCHEM,NEW YORK,NY 10016
来源：
CELL | 1991年 / 65卷 / 03期
基金：
美国国家科学基金会; 美国国家卫生研究院;
关键词：
D O I：
10.1016/0092-8674(91)90457-A
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
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.
引用
收藏
页码：395 / 407
页数：13
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