The BTB domains of the potassium channel tetramerization domain proteins prevalently assume pentameric states

Giovanni Smaldone, Luciano Pirone, Emilia Pedone, Thomas Marlovits, Luigi Vitagliano, Luciano Ciccarelli

Research output: Contribution to journalLetterpeer-review

Abstract

Potassium channel tetramerization domain-containing (KCTD) proteins are involved in fundamental physio-pathological processes. Here, we report an analysis of the oligomeric state of the Bric-à-brack, Tram-track, Broad complex (BTB) domains of seven distinct KCTDs belonging to five major clades of the family evolution tree. Despite their functional and sequence variability, present electron microscopy data highlight the occurrence of well-defined pentameric states for all domains. Our data also show that these states coexist with alternative forms which include open pentamers. Thermal denaturation analyses conducted using KCTD1 as a model suggest that, in these proteins, different domains cooperate to their overall stability. Finally, negative-stain electron micrographs of KCTD6BTB in complex with Cullin3 show the presence of assemblies with a five-pointed pinwheel shape.

Original languageEnglish
Pages (from-to)1663-1671
Number of pages9
JournalFEBS Letters
DOIs
Publication statusPublished - Jun 1 2016

Keywords

  • electron microscopy
  • protein oligomerization
  • protein structure
  • thermal stability

ASJC Scopus subject areas

  • Structural Biology
  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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