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Ssn6-Tup1 global transcriptional co-repressor: Role of the N-terminal glutamine-rich region of Ssn6

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Listed:
  • Athanassios Tartas
  • Christoforos Zarkadas
  • Maria Palaiomylitou
  • Niki Gounalaki
  • Dimitris Tzamarias
  • Metaxia Vlassi

Abstract

The Ssn6-Tup1 complex is a general transcriptional co-repressor formed by the interaction of Ssn6, a tetratricopeptide repeat (TPR) protein, with the Tup1 repressor. We have previously shown that the N-terminal domain of Ssn6 comprising TPRs 1 to 3 is necessary and sufficient for this interaction and that TPR1 plays critical role. In a subsequent study, we provided evidence that in the absence of Tup1, TPR1 is susceptible to proteolysis and that conformational change(s) accompany the Ssn6-Tup1 complex formation. In this study, we address the question whether the N-terminal non-TPR, glutamine-rich tail of Ssn6 (NTpolyQ), plays any role in the Ssn6/Tup1 association. Our biochemical and yeast-two-hybrid data show that truncation/deletion of the NTpolyQ domain of Ssn6 results in its self association and prevents Tup1 interaction. These results combined with in silico modeling data imply a major role of the NTpolyQ tail of Ssn6 in regulating its interaction with Tup1.

Suggested Citation

  • Athanassios Tartas & Christoforos Zarkadas & Maria Palaiomylitou & Niki Gounalaki & Dimitris Tzamarias & Metaxia Vlassi, 2017. "Ssn6-Tup1 global transcriptional co-repressor: Role of the N-terminal glutamine-rich region of Ssn6," PLOS ONE, Public Library of Science, vol. 12(10), pages 1-16, October.
    • Handle: RePEc:plo:pone00:0186363
    DOI: 10.1371/journal.pone.0186363
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    References listed on IDEAS

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    1. Bálint Mészáros & István Simon & Zsuzsanna Dosztányi, 2009. "Prediction of Protein Binding Regions in Disordered Proteins," PLOS Computational Biology, Public Library of Science, vol. 5(5), pages 1-18, May.
    2. Nikolaos Voukkalis & Maria Koutroumani & Christoforos Zarkadas & Eleni Nikolakaki & Metaxia Vlassi & Thomas Giannakouros, 2016. "SRPK1 and Akt Protein Kinases Phosphorylate the RS Domain of Lamin B Receptor with Distinct Specificity: A Combined Biochemical and In Silico Approach," PLOS ONE, Public Library of Science, vol. 11(4), pages 1-21, April.
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