Drosophila melanogaster Paip2 Binds ENY2 and Interacts with the TREX-2 Complex in Histone mRNP Particles

IF 1.5 4区 生物学 Q4 BIOCHEMISTRY & MOLECULAR BIOLOGY Molecular Biology Pub Date : 2024-06-05 DOI:10.1134/s0026893324700146
M. M. Kurshakova, A. N. Krasnov, E. N. Nabirochkina, S. G. Georgieva
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Abstract

ENY2 is an evolutionarily conserved multifunctional protein and is a member of several complexes that regulate various stages of gene expression. ENY2 is a subunit of the TREX-2 complex, which is necessary for the export of bulk mRNA from the nucleus to the cytoplasm through the nuclear pores in many eukaryotes. The wide range of ENY2 functions suggests that it can also associate with other protein factors or complexes. In a search for proteins that interact with ENY2 of Drosophila melanogaster, a cDNA library was screened in a yeast two-hybrid system. ENY2 was thus found to interact with the RNA-binding protein Paip2. Paip2 directly bound ENY2 in vitro and interacted with ENY2 in vivo at the molecular and genetic levels. Paip2 was capable of association with the ENY2-containing TREX-2 complex. Paip2 was present at the locus of the histone gene cluster. Both Paip2 and ENY2 were detected at histone locus body (HLBs), nuclear structure where coordinated histone mRNA transcription and processing take place. Paip2 and subunits of the TREX-2 complex were shown to associate with histone mRNP particles. A Paip2 knockdown via RNA interference resulted in decreased binding of TREX-2 subunits to histone mRNPs. Thus, Paip2 was identified as a new partner protein of ENY2 within the TREX-2 complex and suggested to participate in TREX-2 binding to histone mRNPs.

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黑腹果蝇 Paip2 结合 ENY2 并与组蛋白 mRNP 粒子中的 TREX-2 复合物相互作用
摘要ENY2是一种进化保守的多功能蛋白质,是调节基因表达各个阶段的多个复合体的成员之一。ENY2是TREX-2复合物的一个亚基,在许多真核生物中,TREX-2复合物是将大量mRNA通过核孔从细胞核输出到细胞质所必需的。ENY2功能的广泛性表明,它还能与其他蛋白因子或复合物结合。为了寻找与黑腹果蝇ENY2相互作用的蛋白质,我们在酵母双杂交系统中筛选了一个cDNA文库。结果发现ENY2与RNA结合蛋白Paip2相互作用。Paip2在体外直接与ENY2结合,在体内与ENY2在分子和基因水平上相互作用。Paip2 能够与含有 ENY2 的 TREX-2 复合物结合。Paip2存在于组蛋白基因簇的基因座上。在组蛋白基因座体(HLBs)上检测到了Paip2和ENY2,HLBs是协调组蛋白mRNA转录和加工的核结构。Paip2 和 TREX-2 复合物的亚基与组蛋白 mRNP 颗粒有联系。通过 RNA 干扰敲除 Paip2 会导致 TREX-2 亚基与组蛋白 mRNPs 的结合减少。因此,Paip2 被鉴定为 TREX-2 复合物中 ENY2 的新伙伴蛋白,并被认为参与了 TREX-2 与组蛋白 mRNPs 的结合。
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来源期刊
Molecular Biology
Molecular Biology 生物-生化与分子生物学
CiteScore
1.30
自引率
8.30%
发文量
78
审稿时长
3 months
期刊介绍: Molecular Biology is an international peer reviewed journal that covers a wide scope of problems in molecular, cell and computational biology including genomics, proteomics, bioinformatics, molecular virology and immunology, molecular development biology, molecular evolution and related areals. Molecular Biology publishes reviews, experimental and theoretical works. Every year, the journal publishes special issues devoted to most rapidly developing branches of physical-chemical biology and to the most outstanding scientists.
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