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Issue 7, 2016
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Differential effects of zinc binding on structured and disordered regions in the multidomain STIL protein

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Abstract

Binding of metal ions is an important regulatory mechanism in proteins. Specifically, Zn2+ binding to disordered regions commonly induces a disorder to order transition and gain of structure or oligomerization. Here we show that simultaneous binding of Zn2+ ions has different effects on structured and disordered domains in the same multidomain protein. The centrosomal STIL protein bound Zn2+ ions via both its structured N-terminal domain (NTD) and disordered central region (IDR). Zn2+ binding induced structural rearrangement of the structured NTD but promoted oligomerization of the IDR. We suggest that by binding Zn2+ STIL acquires a different conformation, which allows its oligomerization and induces its activity. Sequence alignment of the oligomerization region revealed a new suggested motif, SxKxS/SxHxS/SxLxS, which may participate in STIL oligomerization. Binding of the same metal ion through a disordered and a structured domain in the same protein is a property that may have implications in regulating the protein activity. By doing so, the protein achieves two parallel outcomes: structural changes and oligomerization that can take place together. Our results describe a new important role of the delicate interplay between structure and intrinsic disorder in proteins.

Graphical abstract: Differential effects of zinc binding on structured and disordered regions in the multidomain STIL protein

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Publication details

The article was received on 10 Jan 2016, accepted on 01 Mar 2016 and first published on 04 Mar 2016


Article type: Edge Article
DOI: 10.1039/C6SC00115G
Citation: Chem. Sci., 2016,7, 4140-4147
  • Open access: Creative Commons BY-NC license
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    Differential effects of zinc binding on structured and disordered regions in the multidomain STIL protein

    H. Amartely, A. David, M. Shamir, M. Lebendiker, S. Izraeli and A. Friedler, Chem. Sci., 2016, 7, 4140
    DOI: 10.1039/C6SC00115G

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