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Biochem Biophys Res Commun. 2017 Jan 22;482(4):1194-1200. doi: 10.1016/j.bbrc.2016.12.011. Epub 2016 Dec 3.

Development of a novel catalytic amyloid displaying a metal-dependent ATPase-like activity.

Author information

1
Laboratorio de Biología Estructural y Molecular, Departamento de Biología, Facultad de Ciencias, Universidad de Chile, Santiago, Chile.
2
Laboratorio de Biología Estructural y Molecular, Departamento de Biología, Facultad de Ciencias, Universidad de Chile, Santiago, Chile. Electronic address: rodrigo.diaz.e@u.uchile.cl.

Abstract

Amyloids are protein aggregates of highly regular structure that are involved in diverse pathologies such as Alzheimer's and Parkinson's disease. Recent evidence has shown that under certain conditions, small peptides can self-assemble into amyloids that exhibit catalytic reactivity towards certain compounds. Here we report a novel peptide with a sequence derived from the active site of RNA polymerase that displays hydrolytic activity towards ATP. The catalytic reaction proceeds in the presence of the divalent metal manganese and the products are ADP and AMP. The kinetic data shows a substrate-dependent saturation of the activity with a maximum rate achieved at around 1 mM ATP. At higher ATP concentrations, we also observed substrate inhibition of the activity. The self-assembly of the peptide into amyloids is strictly metal-dependent and required for the catalysis. Our results show that aspartate-containing amyloids can also be catalysts under conditions that include interactions with metals. Moreover, we show for the first time an amyloid that exerts reactivity towards a biologically essential molecule.

KEYWORDS:

ATP; Amyloid; Catalysis; Hydrolysis; Manganese; Peptide

PMID:
27923655
DOI:
10.1016/j.bbrc.2016.12.011
[Indexed for MEDLINE]

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