Journal article

Functional dissection of an intrinsically disordered protein: Understanding the roles of different domains of Knr4 protein in protein–protein interactions

  • Dagkessamanskaia, Adilia University of Toulouse, Toulouse, France
  • Durand, Fabien University of Toulouse, Toulouse, France
  • Uversky, Vladimir N. Department of Biochemistry and Molecular Biology, Indiana University School of Medicine, Indianapolis, USA - Center for Computational Biology and Bioinformatics, Indiana University School of Medicine, Indianapolis, USA - Institute for Biological Instrumentation, Russian Academy of Sciences, Pushchino, Moscow Region, Russia
  • Binda, Matteo Division of Biochemistry, Department of Medicine, University of Fribourg, Switzerland
  • Lopez, Frédéric INSERM, Toulouse, France
  • Azzouzi, Karim El University of Toulouse, Toulouse, France
  • Francois, Jean Marie University of Toulouse, Toulouse, France
  • Martin-Yken, Hélène University of Toulouse, Toulouse, France
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Published in:
  • Protein Science. - 2010, vol. 19, no. 7, p. 1376–1385
English Knr4, recently characterized as an intrinsically disordered Saccharomyces cerevisiae protein, participates in cell wall formation and cell cycle regulation. It is constituted of a functional central globular core flanked by a poorly structured N-terminal and large natively unfolded C-terminal domains. Up to now, about 30 different proteins have been reported to physically interact with Knr4. Here, we used an in vivo two-hybrid system approach and an in vitro surface plasmon resonance (BIAcore) technique to compare the interaction level of different Knr4 deletion variants with given protein partners. We demonstrate the indispensability of the N-terminal domain of Knr4 for the interactions. On the other hand, presence of the unstructured C-terminal domain has a negative effect on the interaction strength. In protein interactions networks, the most highly connected proteins or “hubs” are significantly enriched in unstructured regions, and among them the transient hub proteins contain the largest and most highly flexible regions. The results presented here of our analysis of Knr4 protein suggest that these large disordered regions are not always involved in promoting the protein–protein interactions of hub proteins, but in some cases, might rather inhibit them. We propose that this type of regions could prevent unspecific protein interactions, or ensure the correct timing of occurrence of transient interactions, which may be of crucial importance for different signaling and regulation processes.
Faculté des sciences et de médecine
Département de Biologie
  • English
Biological sciences
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