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ACS Nano. 2017 Feb 28;11(2):1328-1339. doi: 10.1021/acsnano.6b05992. Epub 2017 Jan 31.

Nanoparticles Associate with Intrinsically Disordered RNA-Binding Proteins.

Author information

1
Department of Biochemistry, Erasmus Medical Center , Rotterdam 3015CE, The Netherlands.
2
Institute of Systematics and Ecology of Animals, SB RAS , Novosibirsk 630091, Russia.

Abstract

Nanoparticles are capable of penetrating cells, but little is known about the way they interact with intracellular proteome. Here we show that inorganic nanoparticles associate with low-complexity, intrinsically disordered proteins from HeLa cytosolic protein extracts in nondenaturing in vitro nanoparticle pull-down assays. Intrinsic protein disorder associates with structural mobility, suggesting that side-chain flexibility plays an important role in the driving of a protein to nanoparticle absorption. Disordered protein domains are often found in a diverse group of RNA-binding proteins. Consequently, the nanoparticle-associated proteomes were enriched in subunits of RNA-processing protein complexes. In turn, this indicates that within a cell, nanoparticles might interfere with protein synthesis triggering a range of cellular responses.

KEYWORDS:

RNA-binding proteins; intrinsically disordered proteins; nanoparticles; proteomics; stress granules

PMID:
28122180
DOI:
10.1021/acsnano.6b05992
[Indexed for MEDLINE]

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