ArticleDoklady. Biochemistry and biophysics2021
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.
Article in Doklady. Biochemistry and biophysics, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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Who cites it
3 citing papers in PubMed, 3 citations in OpenAlex.
- TREX-2-ORC Complex of D. melanogaster Participates in Nuclear Export of Histone mRNA.Doklady. Biochemistry and biophysics · 2024Article
- The Human TREX-2 Complex Interacts with Subunits of the ORC Complex.Doklady. Biochemistry and biophysics · 2023Article
- The Xmas-2 Protein of Drosophila melanogaster Undergoes Cleavage into Two Fragments.Doklady. Biochemistry and biophysics · 2023Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
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Abstract
The TREX-2 protein complex is the key participant in the export of mRNA from the nucleus to the cytoplasm through the nuclear pores. Previously, a protein complex of D. melanogaster consisting of TREX-2 and ORC complexes was purified. It was shown that, in the TREX-2-ORC complex, the Xmas-2 protein, which is the platform for TREX-2 assembly, interacts with the Orc3 protein. The aim of this work was to investigate what regions of the Xmas-2 amino acid sequence are involved in the interaction with Orc3. It was shown that the interaction of Xmas-2 with Orc3 requires a C-terminal region of Xmas-2 located downstream of the CID domain.
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