Journal Article

PUBDB-2017-00420

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png The BTB domains of the potassium channel tetramerization domain proteins prevalently assume pentameric states

Smaldone, G. ; Pirone, L. ; Pedone, E. ; Marlovits, T.CSSB*DESY* ; Vitagliano, L. (Corresponding author) ; Ciccarelli, L. (Corresponding author)CSSB*DESY*

2016
Wiley Chichester

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Please use a persistent id in citations: doi:10.1002/1873-3468.12203

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 KCTD6$^{BTB}$ in complex with Cullin3 show the presence of assemblies with a five-pointed pinwheel shape.

Note: © Federation of European Biochemical Societies ; Post referee fulltext in progress; Embargo 12 months from publication

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Contributing Institute(s):

1. CSSB-UKE (CSSB-UKE)
2. CSSB-UKE-TM (CSSB-UKE-TM)

Research Program(s):

1. 6215 - Soft Matter, Health and Life Sciences (POF3-621) (POF3-621)

Experiment(s):

1. No specific instrument

Appears in the scientific report 2016

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Database coverage:
; BIOSIS Previews ; Current Contents - Life Sciences ; Ebsco Academic Search ; IF < 5 ; JCR ; NCBI Molecular Biology Database ; SCOPUS ; Science Citation Index ; Science Citation Index Expanded ; Thomson Reuters Master Journal List ; Web of Science Core Collection

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