中文摘要：

Telomerase 是包含催化 telomerase 颠倒 transcriptase (TERT ) 和一个 RNA 模板的大 ribonucleoprotein 建筑群。Telomerase 活动被 TERT 表示紧控制，它在 transcriptional 和 translational 以后层次被调整。然而， telomerase 规定和功能的详细分子的机制充分没被理解。识别贡献 telomerase 规定的余因子，我们采用了酵母为交往 hTERT 蛋白质屏蔽的二混血儿的系统，用是的 hTERT T 主题诱饵。我们作为一个新奇 hTERT 相互作用搭挡识别 C53。我们证明 C53 在 vivo 并且在 vitro 与 hTERT 交往。C53 弄空增加 telomerase 活动，和 C53 overexpression 在 MCF7 房间禁止 telomerase 活动。另外， C53 白氨酸拉链领域(氨基酸 301400 ) 为和 hTERT 的相互作用被要求。删除白氨酸拉链领域与 hTERT 消除 C53 相互作用并且在 telomerase 活动废除它的禁止的效果。一起拿，我们的结果证明 C53 是否定地调整 telomerase 的新奇联系 hTERT 的蛋白质活动。

英文摘要：

Telomerase is a large ribonucleoprotein complex that contains a catalytic telomerase reverse trans criptase （TERT） and an RNA template. Telomerase activity is tightly controlled by TERT expression, which is regulated at both the transcriptional and post-translational levels. However, the detailed molecular mechanisms of telomerase regulation and function are not fully understood. To identify cofactors that contribute to telomerase regulation, we employed a yeast two-hybrid system to screen for hTERT-interacting proteins, using the hTERT T-motif as bait. We identify C53 as a novel hTERT interaction partner. We show that C53 interacts with hTERT both in vivo and in vitro. C53 depletion increases telomerase activity, and C53 overexpression inhibits telomerase activity in MCF7 cells. In addition, the C53 leucine zipper domain （amino acids 301-400） is required for interaction with hTERT. Deleting the leucine zipper domain eliminates C53 interaction with hTERT and abrogates its inhibitory effect on telomerase activity. Taken together, our results demonstrate that C53 is a novel hTERT-associated protein that negatively regulates telomerase activity.