The Xmas-2 Homologues, the Main Component of the TREX-2 mRNA Export Complex.
TREX-2
Xmas-2
mRNA export
transcription
Journal
Doklady. Biochemistry and biophysics
ISSN: 1608-3091
Titre abrégé: Dokl Biochem Biophys
Pays: United States
ID NLM: 101126895
Informations de publication
Date de publication:
Nov 2020
Nov 2020
Historique:
received:
17
07
2020
accepted:
10
08
2020
revised:
10
08
2020
entrez:
28
12
2020
pubmed:
29
12
2020
medline:
1
7
2021
Statut:
ppublish
Résumé
TREX-2 complex is responsible for general mRNA export from nucleus to cytoplasm in eukaryote. The main protein of TREX-2 complex of D. melanogaster is protein Xmas-2. Its homologues in yeast and humans are Sac3 and GANP proteins, respectively. All three proteins contain the highly conserved domain Sac3-GANP, which is essential for interaction of TREX-2 complex with mRNA and another protein of the complex, PCID2. We identified two Xmas-2 homologues in D. melanogaster using the Sac3-GANP family domain sequence. These proteins have a common domain responsible for interaction with the PCID2 protein and RNA and are present in other eukaryotes. The function of these proteins is unknown. However, on the basis of their structural organization, we can assume that they interact with nucleic acids.
Identifiants
pubmed: 33368044
doi: 10.1134/S1607672920060101
pii: 10.1134/S1607672920060101
doi:
Substances chimiques
Drosophila Proteins
0
RNA, Messenger
0
RNA-Binding Proteins
0
xmas protein, Drosophila
0
Exodeoxyribonucleases
EC 3.1.-
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
325-328Références
Fischer, T., Strasser, K., Racz, A., Rodriguez-Navarro, S., Oppizzi, M., Ihrig, P., Lechner, J., and Hurt, E., EMBO J., 2002, vol. 21, no. 21, pp. 5843–5852.
doi: 10.1093/emboj/cdf590
Kurshakova, M.M., Krasnov, A.N., Kopytova, D.V., Shidlovskii, Y.V., Nikolenko, J.V., Nabirochkina, E.N., Spehner, D., Schultz, P., Tora, L., and Georgieva, S.G., EMBO J., 2007, vol. 26, no. 24, pp. 4956–4965.
doi: 10.1038/sj.emboj.7601901
Lu, Q., Tang, X., Tian, G., Wang, F., Liu, K., Nguyen, V., Kohalmi, S.E., Keller, W.A., Tsang, E.W.T., Harada, J.J., Rothstein, S.J., and Cui, Y., Plant J. Cell Mol. Biol., 2010, vol. 61, no. 2, pp. 259–270.
Ellisdon, A.M., Dimitrova, L., Hurt, E., and Stewart, M., Nat. Struct. Mol. Biol., 2012, vol. 19, no. 3, pp. 328–336.
doi: 10.1038/nsmb.2235
Jani, D., Lutz, S., Marshall, N.J., Fischer, T., Kohler, A., Ellisdon, A.M., Hurt, E., and Stewart, M., Mol. Cell, 2009, vol. 33, no. 6, pp. 727–737.
doi: 10.1016/j.molcel.2009.01.033
Wickramasinghe, V.O., Stewart, M., and Laskey, R.A., Nucleus (Austin, Tex.), 2010, vol. 1, no. 5, pp. 393–396.
Jani, D., Valkov, E., and Stewart, M., Nucleic Acids Res., 2014, vol. 42, no. 10, pp. 6686–6697.
doi: 10.1093/nar/gku252
Kopytova, D.V., Il’in, Yu.V., and Nabirochkina, E.N., Dokl. Biochem. Biophys., 2018, vol. 479, pp. 87–89.
doi: 10.1134/S1607672918020102
Liu, A.-G., Zhong, J.-C., Chen, G., He, R.-Q., He, Y.-Q., Ma, J., Yang, L.-H., Wu, X.-J., Huang, J.-T., Li, J.-J., Mo, W.-J., and Qin, X.-G., Int. J. Oncol., 2020, vol. 57, no. 1, pp. 122–138.
pubmed: 32319600
pmcid: 7252452
Wang, X., Li, G., Luo, Q., and Gan, C., Oncol. Lett., 2018, vol. 15, no. 6, pp. 8983–8990.
pubmed: 29844815
pmcid: 5958829
Fan, J., Yan, D., Teng, M., Tang, H., Zhou, C., Wang, X., Li, D., Qiu, G., and Peng, Z., Clin. Cancer Res., 2011, vol. 17, no. 9, pp. 2908–2918.
doi: 10.1158/1078-0432.CCR-10-2552