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首页> 外文期刊>Molecular and Cellular Biology >A CPSF-73 Homologue Is Required for Cell Cycle Progression but Not Cell Growth and Interacts with a Protein Having Features of CPSF-100
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A CPSF-73 Homologue Is Required for Cell Cycle Progression but Not Cell Growth and Interacts with a Protein Having Features of CPSF-100

机译：CPSF-73同源物是细胞周期发展所必需的，而不是细胞生长所必需的，并且与具有CPSF-100特征的蛋白质相互作用

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Formation of the mature 3′ ends of the vast majority of cellular mRNAs occurs through cleavage and polyadenylation and requires a cleavage and polyadenylation specificity factor (CPSF) containing, among other proteins, CPSF-73 and CPSF-100. These two proteins belong to a superfamily of zinc-dependent β-lactamase fold proteins with catalytic specificity for a wide range of substrates including nucleic acids. CPSF-73 contains a zinc-binding histidine motif involved in catalysis in other members of the β-lactamase superfamily, whereas CPSF-100 has substitutions within the histidine motif and thus is unlikely to be catalytically active. Here we describe two previously unknown human proteins, designated RC-68 and RC-74, which are related to CPSF-73 and CPSF-100 and which form a complex in HeLa and mouse cells. RC-68 contains the intact histidine motif, and hence it might be a functional counterpart of CPSF-73, whereas RC-74 lacks this motif, thus resembling CPSF-100. In HeLa cells RC-68 is present in both the cytoplasm and the nucleus whereas RC-74 is exclusively nuclear. RC-74 does not interact with CPSF-73, and neither RC-68 nor RC-74 is found in a complex with CPSF-160, indicating that these two proteins form a separate entity independent of the CPSF complex and are likely involved in a pre-mRNA processing event other than cleavage and polyadenylation of the vast majority of cellular pre-mRNAs. RNA interference-mediated depletion of RC-68 arrests HeLa cells early in G1 phase, but surprisingly the arrested cells continue growing and reach the size typical of G2 cells. RC-68 is highly conserved from plants to humans and may function in conjunction with RC-74 in the 3′ end processing of a distinct subset of cellular pre-mRNAs encoding proteins required for G1 progression and entry into S phase.
机译：绝大多数细胞mRNA的成熟3'末端的形成是通过切割和聚腺苷酸化来实现的，并且需要包含CPSF-73和CPSF-100等蛋白质的切割和聚腺苷酸化特异性因子（CPSF）。这两种蛋白属于锌依赖性β-内酰胺酶折叠蛋白的超家族，其对包括核酸在内的多种底物具有催化特异性。 CPSF-73在β-内酰胺酶超家族的其他成员中包含与催化有关的锌结合组氨酸基序，而CPSF-100在组氨酸基序内具有取代基，因此不太可能具有催化活性。在这里，我们描述了两个以前未知的人类蛋白质，称为RC-68和RC-74，它们与CPSF-73和CPSF-100相关，并在HeLa和小鼠细胞中形成复合物。 RC-68包含完整的组氨酸基序，因此它可能是CPSF-73的功能对应物，而RC-74缺少此基序，因此类似于CPSF-100。在HeLa细胞中，RC-68存在于细胞质和细胞核中，而RC-74仅存在于细胞核中。 RC-74不与CPSF-73相互作用，并且在与CPSF-160形成的复合物中均未找到RC-68和RC-74，这表明这两种蛋白质形成了独立于CPSF复合物的独立实体，可能与除大多数细胞前mRNA的裂解和聚腺苷酸化以外，前mRNA加工事件。 RNA干扰介导的RC-68耗竭在G 1 早期阻滞HeLa细胞，但令人惊讶的是，被阻滞的细胞继续生长并达到G 2 细胞的典型大小。 RC-68从植物到人类都是高度保守的，并且可能与RC-74一起在编码G 1 进程和进入所需蛋白的细胞前mRNA的不同子集的3'末端加工中发挥作用进入S期。

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