中文摘要：

在象它在各种各样的原子进程的函数一样的原子核的肌动朊的存在在过去几年里被弄明白。肌动朊被知道是部分改变 ofchromatin 建筑群 BAF，它为 BAF 建筑群的 Brg1component 的最大的 ATPase 活动被要求。而且，在抄写的肌动朊的必要角色调停了 byRNA 聚合酶Ⅰ，Ⅱ和Ⅲ最近被表明了。在另一方面，肌浆球蛋白Ⅰ i 形式，为原子核本地化包含唯一的 NH2 终端延期，因此在原子核是明确地局部性的。这是众所周知的，肌浆球蛋白Ⅰ是 acttn 有约束力的蛋白质并且在各种各样的细胞的活动起一个重要作用。不过肌动朊和原子肌浆球蛋白Ⅰ(NM Ⅰ) 被含有在基因表示起不同作用，没有证据因为可能涉及基因抄写的 theactin 肌浆球蛋白相互作用由 RNA Ⅱ(RNAP Ⅱ) 调停了。这里，我们显示出肌动朊和 NM Ⅰ被使用合作本地化在原子核与 RNAP Ⅱ联系， co-IP 试金，和他们可以对基因抄写一起起作用的证据。对β - 肌动朊或 NM Ⅰ的 Theantibodies 能堵住 RNA 合成在一在有包括倡导者和人的 autocrine motilltyfactor 的编码区域的模板 DNA 的 vitro 抄写系统真核细胞受体(hAMFR ) 基因；抗体与净化的肌动朊和 NM Ⅰ预先吸附没在 transcriptional 抑制有效果，显示由 anti-actinand anti-NM Ⅰ的抄写的抑制是特定的。这些结果在调整抄写建议肌动朊肌浆球蛋白建筑群的直接参与。肌动朊和 NM Ⅰ可以在 RNAP Ⅱ - 与 RNAP Ⅱ和和肌动朊和 NM Ⅰ功能的 RNAP Ⅱ的相互作用在一样的建筑群共存，这也含有调停的抄写。

英文摘要：

The presence of actin in the nucleus as well as its functions in various nuclear processes has been made clear in the past few years. Actin is known to be a part of chromatin-remodeling complexes BAF, which are required for maximal ATPase activity of the Brgl component of the BAF complex. Moreover, the essential roles of actin in transcription mediated by RNA polymerases Ⅰ, Ⅱ and Ⅲ have been demonstrated recently. On the other hand, a myosin Ⅰ isoform, which contains a unique NH2-terminal extension for nucleus localization, has been specifically localized in nucleus. As is well known, myosin Ⅰ is an actin-binding protein and plays an important role in various cellular activities. Though actin and nuclear myosin Ⅰ （NM Ⅰ） have been implicated to play distinct roles in gene expression, there has been no evidence for the actin-myosin interaction that might be involved in gene transcription mediated by RNA polymerase Ⅱ （RNAP Ⅱ）. Here we show evidence that both actin and NM Ⅰ are associated with RNAP Ⅱ in nucleus by using co-localization and co-IP assays, and they may act together on gene transcription. The antibodies against β-actin or NM Ⅰ can block RNA synthesis in a eukaryotic in vitro transcription system with template DNA comprising the promoter and the coding region of human autocrine motility factor receptor （hAMFR） gene; the antibodies pre-adsorbed with purified actin and NM Ⅰ have no effect in transcriptional inhibition, indicating that the inhibition of transcription by anti-actin and anti-NM b is specific. These results suggest a direct involvement of actin-myosin complexes in regulating transcription. It also implicates that actin and NMⅠ may co-exist in a same complex with RNAP Ⅱ and the interaction of RNAP Ⅱ with actin and NM Ⅰ functions in the RNAP Ⅱ-mediated transcription.