THE XMAS-2 PROTEIN OF  DROSOPHILA MELANOGASTER  UNDERGOES CLEAVAGE INTO TWO FRAGMENTS

M. M. Kurshakova; Куршакова М. М.; S. G. Georgieva; Георгиева С. Г.; D. V. Kopytova; Копытова Д. В.

doi:10.31857/S2686738922700111

THE XMAS-2 PROTEIN OF DROSOPHILA MELANOGASTER UNDERGOES CLEAVAGE INTO TWO FRAGMENTS

Authors: Kurshakova M.M.¹, Georgieva S.G.¹, Kopytova D.V.¹
Affiliations:
1. Institute of Molecular Biology, Russian Academy of Sciences
Issue: Vol 509, No 1 (2023)
Pages: 166-169
Section: Articles
URL: https://journals.rcsi.science/2686-7389/article/view/135642
DOI: https://doi.org/10.31857/S2686738922700111
EDN: https://elibrary.ru/NAZLMZ
ID: 135642

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Abstract
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Abstract

The TREX-2 complex integrates several stages of gene expression, such as transcriptional activation and mRNA export. In D. melanogaster TREX-2 consists of four main proteins: Xmas-2, ENY2, PCID2, and Sem1p. Xmas-2 protein is the core subunit of the complex with which other TREX-2 subunits interact. Xmas-2 homologues have been found in all higher eukaryotes. Previously, it was shown that the human Xmas-2 homologue, GANP protein can undergo cleavage into two parts, probably during apoptotic cell death. We showed that the Xmas-2 protein of D. melanogaster also can split into two fragments. The resulting fragments of the protein correspond to the two large domains of Xmas-2. Protein splitting is observed both in vivo and in vitro. However, Xmas-2 cleavage in D. melanogaster is observed under normal conditions and is probably a part of the mechanism of transcription and mRNA export regulation in D. melanogaster.

Keywords

TREX-2, Xmas-2, mRNA export, transcription

References

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