Preprint Article Version 1 This version is not peer-reviewed

An Amyloidogenic Sequence at the N-Terminus of the Androgen Receptor Impacts Polyglutamine Aggregation

Version 1 : Received: 16 May 2017 / Approved: 16 May 2017 / Online: 16 May 2017 (17:48:54 UTC)

A peer-reviewed article of this Preprint also exists.

Oppong, E.; Stier, G.; Gaal, M.; Seeger, R.; Stoeck, M.; Delsuc, M.-A.; Cato, A.C.B.; Kieffer, B. An Amyloidogenic Sequence at the N-Terminus of the Androgen Receptor Impacts Polyglutamine Aggregation. Biomolecules 2017, 7, 44. Oppong, E.; Stier, G.; Gaal, M.; Seeger, R.; Stoeck, M.; Delsuc, M.-A.; Cato, A.C.B.; Kieffer, B. An Amyloidogenic Sequence at the N-Terminus of the Androgen Receptor Impacts Polyglutamine Aggregation. Biomolecules 2017, 7, 44.

Journal reference: Biomolecules 2017, 7, 44
DOI: 10.3390/biom7020044

Abstract

The human androgen receptor (AR) is a ligand inducible transcription factor harboring an amino terminal domain (AR-NTD) hosting the ligand independent activation function. AR-NTD is intrinsically disordered and display aggregation properties conferred by the presence of a poly-glutamine (polyQ) sequence of 22 residues. The length of the polyQ sequence, as well as the presence of adjacent sequence motifs modulate this aggregation property. AR-NTD contains also a conserved sequence motif KELCKAVSVSM that displays an intrinsic property to form amyloid fibrils under mild oxidative conditions of its conserved cysteine residue. As peptide sequences with intrinsic ability to oligomerize are reported to have an impact on the aggregation of polyQ tract, we determined the effect of the KELCKAVSVSM on the polyQ stretch in the context of the AR NTD, using Atomic Force Microscopy (AFM). Here, we present evidence for a crosstalk between the amyloidogenic properties of the KELCKAVSVSM motif and the polyQ stretch at the AR NTD.

Subject Areas

amyloid peptides; androgen receptor; nuclear receptor; aggregation; atomic force microscopy

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