Reconstitution of the CstF complex unveils a regulatory role for CstF-50 in recognition of 3'-end processing signals.

Reconstitution of the CstF complex unveils a regulatory role for CstF-50 in recognition of 3'-end processing signals.
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CSTF复合体的重建揭示了CSTF-50在识别3'-End处理信号方面的调节作用。

DOI:
10.1093/nar/gkx1177
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发表时间:
2018-01-25
影响因子:
14.9
通讯作者:
Varani G
Varani G
中科院分区:
生物学2区
文献类型:
--
作者:
Yang W;Hsu PL;Yang F;Song JE;Varani G

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裂解刺激因子(CstF)是一种高度保守的蛋白质复合物,由三个亚基组成,可识别真核mrna多聚腺苷化信号下游的富含G/ u的序列。虽然CstF在25年前就被发现,但每个亚基的结构和对RNA识别的贡献尚未完全了解。在本研究中,我们为CstF-50通过与CstF-77的相互作用募集到CstF提供了结构基础,并建立了CstF的六聚体组装为靶向各种富含G/ u的序列提供了高亲和力的平台。我们进一步证明,CstF-77增强了CstF-64 RRM对RNA靶标的亲和力,而CstF-50精细调节了复合物识别特定长度和内容的G/U序列的能力。
Cleavage stimulation factor (CstF) is a highly conserved protein complex composed of three subunits that recognizes G/U-rich sequences downstream of the polyadenylation signal of eukaryotic mRNAs. While CstF has been identified over 25 years ago, the architecture and contribution of each subunit to RNA recognition have not been fully understood. In this study, we provide a structural basis for the recruitment of CstF-50 to CstF via interaction with CstF-77 and establish that the hexameric assembly of CstF creates a high affinity platform to target various G/U-rich sequences. We further demonstrate that CstF-77 boosts the affinity of the CstF-64 RRM to the RNA targets and CstF-50 fine tunes the ability of the complex to recognize G/U sequences of certain lengths and content.
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