灵鹊做题网英语翻译Importantly,ectopic TRF1 expression cannot complement fo
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英语翻译
Importantly,ectopic TRF1 expression cannot complement for the loss of TRF2,as frequent DNA-damage foci at telomeres—termed telomere-induced foci (TIF)—and chromosome end-to-end fusions still appear (Fig.1b–d).Conversely,a TRF2 construct that lacks the N-terminal basic domain (TRF2ΔB) is able to suppress TIF formation and end-to-end chromosome fusions (Fig.1b–d).Similarly,a TRF2 construct in which the DNA-binding domain was replaced with the TRF1 MYB domain (TRFcM) can complement for loss of TRF2 (Fig.1b–d).These data show that,in vivo,the specific ability of TRF2 to protect chromosome ends cannot be explained by a specificity of its DNA-binding domain,or by its unique N-terminal basic domain.By contrast,both the TRFH domain and the hinge domain of TRF2 are required to prevent the initial steps in the DDR pathway,as assessed by γH2AX localization at telomeres in cells expressing a construct containing either the TRFH domain (TRFcT) or the hinge domain (TRFcH) of TRF1 (Fig.1b,c).Interestingly,we found that localization of TRFcT at telomeres is sufficient to inhibit the recruitment of key mediators of the DDR pathway downstream of
Importantly,ectopic TRF1 expression cannot complement for the loss of TRF2,as frequent DNA-damage foci at telomeres—termed telomere-induced foci (TIF)—and chromosome end-to-end fusions still appear (Fig.1b–d).Conversely,a TRF2 construct that lacks the N-terminal basic domain (TRF2ΔB) is able to suppress TIF formation and end-to-end chromosome fusions (Fig.1b–d).Similarly,a TRF2 construct in which the DNA-binding domain was replaced with the TRF1 MYB domain (TRFcM) can complement for loss of TRF2 (Fig.1b–d).These data show that,in vivo,the specific ability of TRF2 to protect chromosome ends cannot be explained by a specificity of its DNA-binding domain,or by its unique N-terminal basic domain.By contrast,both the TRFH domain and the hinge domain of TRF2 are required to prevent the initial steps in the DDR pathway,as assessed by γH2AX localization at telomeres in cells expressing a construct containing either the TRFH domain (TRFcT) or the hinge domain (TRFcH) of TRF1 (Fig.1b,c).Interestingly,we found that localization of TRFcT at telomeres is sufficient to inhibit the recruitment of key mediators of the DDR pathway downstream of
重要的是,异位TRF1表达不能补充TRF2的损失,因为频繁的DNA损伤病灶在端粒被称为端粒的致灶（TIF）和染色体端-端融合仍出现（图1b–D）.相反,一个TRF2构造,缺乏的N-末端的基本域（TRF2ΔB）能够抑制TIF形成和端到端的染色体融合（图1b–D）.同样的,在其中的DNA结合结构域与TRF1 MYB结构域替换构建TRF2（trfcm）可以损失的TRF2补体（图1b–D）.这些数据表明,在体内,TRF2保护染色体末端的特殊能力不能被特异性的DNA结合结构域的解释,或通过其独特的N-端基本域.相比之下,两TRFH域和TRF2铰链域必须防止在DDR通路的初始步骤,评估γH2AX定位在表达构建体含有TRFH域细胞的端粒（trfct）或铰链的域（trfch TRF1（图1b）,C）.有趣的是,我们发现trfct在端粒的定位是足以抑制下游的DDR通路的关键介质的招聘
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