ArticleNucleic acids research2016
ORC interacts with THSC/TREX-2 and its subunits promote Nxf1 association with mRNP and mRNA export in Drosophila.
Article in Nucleic acids research, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 37 citations in OpenAlex.
- Local RNA Structure, not Primary Sequence, Governs the Binding Specificity of PCID2 in Drosophila melanogaster.Doklady. Biochemistry and biophysics · 2026Article
- ENY2 Protein Is Present at the Histone Locus Body HLB As Part of Complexes with Different Functions in Transcription and mRNA Export.Doklady. Biochemistry and biophysics · 2026Article
- TREX-2 mRNA Export Complex Interacts with HLB Component FLASH and Is Recruited to Processed Histone mRNAs.Doklady. Biochemistry and biophysics · 2025Article
- Nup153 and TPR/Megator Interact with TREX-2 Subunits and Are Essential for TREX-2-Dependent Nuclear Export ofInternational journal of molecular sciences · 2025Article
- Interdomain Interactions of the PCID2 Protein, One of the Subunits of the TREX-2 mRNA Export Complex in Drosophila melanogaster.Doklady. Biochemistry and biophysics · 2025Article
- Two RNA-Binding Regions of PCID2, a Subunit of the TREX-2 mRNA Nuclear Export Complex, Competitively Interact with the 3' Noncoding Region of ras2 mRNA.Doklady. Biochemistry and biophysics · 2025Article
- Point Mutations in the M Domain of PCID2 Impair Its Function in mRNA Export in Drosophila melanogaster.Doklady biological sciences : proceedings of the Academy of Sciences of the USSR, Biological sciences sections · 2024Article
- TREX-2-ORC Complex of D. melanogaster Participates in Nuclear Export of Histone mRNA.Doklady. Biochemistry and biophysics · 2024Article
- Interaction of mRNA with the C-Terminal Domain of PCID2, a Subunit of the TREX-2 Complex, Is Required for Its Export from the Nucleus to the Cytoplasm in Drosophila melanogaster.Doklady. Biochemistry and biophysics · 2023Article
- The Human TREX-2 Complex Interacts with Subunits of the ORC Complex.Doklady. Biochemistry and biophysics · 2023Article
- DNA mimic foldamers affect chromatin composition and disturb cell cycle progression.Nucleic acids research · 2023Article
- ORC1 binds to cis-transcribed RNAs for efficient activation of replication origins.Nature communications · 2023Article
- PCID2 Subunit of theCurrent issues in molecular biology · 2023Article
- The Xmas-2 Protein of Drosophila melanogaster Undergoes Cleavage into Two Fragments.Doklady. Biochemistry and biophysics · 2023Article
- Distinct roles of Arabidopsis ORC1 proteins in DNA replication and heterochromatic H3K27me1 deposition.Nature communications · 2023Article
- PCID2, a subunit of theRNA biology · 2021Article
- The RNA-Binding Protein SBR (Dm NXF1) Is Required for the Constitution of Medulla Boundaries inCells · 2021Article
- Study of the Interaction between Xmas-2, the Main Protein of TREX-2 mRNA Export Complex, and the Orc3 Protein, a Subunit of ORC Complex of D. melanogaster.Doklady. Biochemistry and biophysics · 2021Article
- Novel candidate biomarkers of origin recognition complex 1, 5 and 6 for survival surveillance in patients with hepatocellular carcinoma.Journal of Cancer · 2020Article
- Identification of the ORC Complex Subunits That Can Interact with the ENY2 Protein of Drosophila melanogaster.Doklady. Biochemistry and biophysics · 2018Article
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The origin recognition complex (ORC) of eukaryotes associates with the replication origins and initiates the pre-replication complex assembly. In the literature, there are several reports of interaction of ORC with different RNAs. Here, we demonstrate for the first time a direct interaction of ORC with the THSC/TREX-2 mRNA nuclear export complex. The THSC/TREX-2 was purified from the Drosophila embryonic extract and found to bind with a fraction of the ORC. This interaction occurred via several subunits and was essential for Drosophila viability. Also, ORC was associated with mRNP, which was facilitated by TREX-2. ORC subunits interacted with the Nxf1 receptor mediating the bulk mRNA export. The knockdown of Orc5 led to a drop in the Nxf1 association with mRNP, while Orc3 knockdown increased the level of mRNP-bound Nxf1. The knockdown of Orc5, Orc3 and several other ORC subunits led to an accumulation of mRNA in the nucleus, suggesting that ORC participates in the regulation of the mRNP export.
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