Analysis of the Nse3/MAGE-binding domain of the Nse4/EID family proteins
Jazyk angličtina Země Spojené státy americké Médium print-electronic
Typ dokumentu časopisecké články, práce podpořená grantem
PubMed
22536443
PubMed Central
PMC3335016
DOI
10.1371/journal.pone.0035813
PII: PONE-D-11-25611
Knihovny.cz E-zdroje
- MeSH
- chromozomální proteiny, nehistonové MeSH
- inhibitor diferenciace 2 MeSH
- interakční proteinové domény a motivy MeSH
- intracelulární signální peptidy a proteiny chemie genetika metabolismus MeSH
- jaderné proteiny chemie MeSH
- konzervovaná sekvence MeSH
- lidé MeSH
- molekulární modely MeSH
- molekulární sekvence - údaje MeSH
- mutageneze cílená MeSH
- peptidové fragmenty chemie genetika metabolismus MeSH
- počítačová simulace MeSH
- proteiny buněčného cyklu genetika metabolismus MeSH
- rekombinantní proteiny chemie genetika metabolismus MeSH
- Schizosaccharomyces pombe - proteiny chemie MeSH
- Schizosaccharomyces MeSH
- sekvence aminokyselin MeSH
- substituce aminokyselin MeSH
- techniky dvojhybridového systému MeSH
- transportní proteiny chemie genetika metabolismus MeSH
- vazba proteinů MeSH
- Check Tag
- lidé MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Názvy látek
- chromozomální proteiny, nehistonové MeSH
- EID2 protein, human MeSH Prohlížeč
- EID3 protein, human MeSH Prohlížeč
- inhibitor diferenciace 2 MeSH
- intracelulární signální peptidy a proteiny MeSH
- jaderné proteiny MeSH
- Nse3 protein, S pombe MeSH Prohlížeč
- Nse4 protein, S pombe MeSH Prohlížeč
- NSMCE3 protein, human MeSH Prohlížeč
- peptidové fragmenty MeSH
- proteiny buněčného cyklu MeSH
- rekombinantní proteiny MeSH
- Schizosaccharomyces pombe - proteiny MeSH
- SMC5 protein, human MeSH Prohlížeč
- transportní proteiny MeSH
BACKGROUND: The Nse1, Nse3 and Nse4 proteins form a tight sub-complex of the large SMC5-6 protein complex. hNSE3/MAGEG1, the mammalian ortholog of Nse3, is the founding member of the MAGE (melanoma-associated antigen) protein family and the Nse4 kleisin subunit is related to the EID (E1A-like inhibitor of differentiation) family of proteins. We have recently shown that human MAGE proteins can interact with NSE4/EID proteins through their characteristic conserved hydrophobic pocket. METHODOLOGY/PRINCIPAL FINDINGS: Using mutagenesis and protein-protein interaction analyses, we have identified a new Nse3/MAGE-binding domain (NMBD) of the Nse4/EID proteins. This short domain is located next to the Nse4 N-terminal kleisin motif and is conserved in all NSE4/EID proteins. The central amino acid residues of the human NSE4b/EID3 domain were essential for its binding to hNSE3/MAGEG1 in yeast two-hybrid assays suggesting they form the core of the binding domain. PEPSCAN ELISA measurements of the MAGEC2 binding affinity to EID2 mutant peptides showed that similar core residues contribute to the EID2-MAGEC2 interaction. In addition, the N-terminal extension of the EID2 binding domain took part in the EID2-MAGEC2 interaction. Finally, docking and molecular dynamic simulations enabled us to generate a structure model for EID2-MAGEC2. Combination of our experimental data and the structure modeling showed how the core helical region of the NSE4/EID domain binds into the conserved pocket characteristic of the MAGE protein family. CONCLUSIONS/SIGNIFICANCE: We have identified a new Nse4/EID conserved domain and characterized its binding to Nse3/MAGE proteins. The conservation and binding of the interacting surfaces suggest tight co-evolution of both Nse4/EID and Nse3/MAGE protein families.
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