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首页> 外文期刊>Molecular and Cellular Biology >Asymmetric Recognition of Nonconsensus AP-1 Sites by Fos-Jun and Jun-Jun Influences Transcriptional Cooperativity with NFAT1
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Asymmetric Recognition of Nonconsensus AP-1 Sites by Fos-Jun and Jun-Jun Influences Transcriptional Cooperativity with NFAT1

机译：Fos-Jun和Jun-Jun对非共识AP-1位点的不对称识别影响转录与NFAT1的协同作用。

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Many regulatory elements in eukaryotic promoters do not correspond to optimal recognition sequences for the transcription factors that regulate promoter function by binding to the elements. The sequence of the binding site may influence the structural and functional properties of regulatory protein complexes. Fos-Jun heterodimers were found to bind nonconsensus AP-1 sites in a preferred orientation. Oriented Fos-Jun heterodimer binding was attributed to nonidentical recognition of the two half-sites by Fos and Jun. Jun bound preferentially to the consensus half-site, whereas Fos was able to bind nonconsensus half-sites. The orientation of heterodimer binding affected the transcriptional cooperativity of Fos-Jun-NFAT1 complexes at composite regulatory elements in mammalian cells. Jun dimerization with Fos versus ATF2 caused it to bind opposite half-sites at nonconsensus AP-1 elements. Similarly, ATF2 bound to opposite half-sites in Fos-ATF2-NFAT1 and ATF2-Jun-NFAT1 complexes. The orientations of nonconsensus AP-1 sites within composite regulatory elements affected the cooperativity of Fos-Jun as well as Jun-Jun binding with NFAT1. Since Jun homodimers cannot bind to AP-1 sites in a preferred orientation, the effects of the orientations of nonconsensus AP-1 sites on the stabilities of Jun-Jun-NFAT1 complexes are likely to be due to asymmetric conformational changes in the two subunits of the homodimer. Nonconsensus AP-1 site orientation also affected the synergy of transcription activation between Jun homodimers and NFAT1 at composite regulatory elements. The asymmetric recognition of nonconsensus AP-1 sites can therefore influence the transcriptional activities of Fos and Jun both through effects on the orientation of heterodimer binding and through differential conformational changes in the two subunits of the dimer.
机译：真核启动子中的许多调节元件并不对应于通过结合启动子来调节启动子功能的转录因子的最佳识别序列。结合位点的序列可能影响调节蛋白复合物的结构和功能特性。发现Fos-Jun异二聚体以优选方向结合非共识AP-1位点。定向的Fos-Jun异二聚体结合归因于Fos和Jun.Jun对两个半位点的不同识别，而Jun优先结合共识的半位点，而Fos能够结合非共识的半位点。异二聚体结合的方向影响哺乳动物细胞中复合调控元件上Fos-Jun-NFAT1复合物的转录协同性。用Fos与ATF2进行的Jun二聚化导致其在非共识AP-1元件处结合相对的半位。同样，ATF2结合到Fos-ATF2-NFAT1和ATF2-Jun-NFAT1复合物中相对的半位。复合调控元件内非共识AP-1位点的方向影响了Fos-Jun的协同作用以及Jun-Jun与NFAT1的结合。由于Jun同二聚体不能以优选的方向与AP-1位点结合，因此非一致的AP-1位点的方向对Jun-Jun-NFAT1复合物稳定性的影响很可能是由于两个亚基的不对称构象变化所致。同型二聚体。不一致的AP-1位点方向还影响Jun同源二聚体与NFAT1在复合调控元件上的转录激活协同作用。因此，非共识AP-1位点的不对称识别可通过影响异二聚体结合的方向以及通过二聚体两个亚基的差异构象变化来影响Fos和Jun的转录活性。

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