Utilizing split-NanoLuc luciferase fragments as luminescent probes for protein solubility in living cells.


Journal

Methods in enzymology
ISSN: 1557-7988
Titre abrégé: Methods Enzymol
Pays: United States
ID NLM: 0212271

Informations de publication

Date de publication:
2019
Historique:
pmc-release: 09 03 2020
entrez: 4 6 2019
pubmed: 4 6 2019
medline: 23 2 2020
Statut: ppublish

Résumé

Protein misfolding and aggregation is now recognized as a hallmark of numerous human diseases. Standard bioanalytical techniques for monitoring protein aggregation generally rely on small molecules that provide an optical readout of fibril formation. While these methods have been useful for mechanistic studies, additional approaches are required to probe the equilibrium between soluble and insoluble protein within living systems. Such approaches could provide platforms for the identification of inhibitors of protein aggregation as well as a means to investigate the effect of mutations on protein aggregation in model systems. In this chapter, we provide detailed protocols for employing split-NanoLuc luciferase (Nluc) fragments to monitor changes in protein solubility in bacterial and mammalian cells. This sensitive luminesce-based assay can report upon changes in protein solubility induced by inhibitors and disease-relevant mutations.

Identifiants

pubmed: 31155065
pii: S0076-6879(19)30022-9
doi: 10.1016/bs.mie.2019.02.003
pmc: PMC6567984
mid: NIHMS1033950
pii:
doi:

Substances chimiques

Luminescent Agents 0
Protein Aggregates 0
Proteins 0
Luciferases EC 1.13.12.-

Types de publication

Journal Article Research Support, N.I.H., Extramural

Langues

eng

Sous-ensembles de citation

IM

Pagination

55-66

Subventions

Organisme : NIGMS NIH HHS
ID : R35 GM119751
Pays : United States

Informations de copyright

© 2019 Elsevier Inc. All rights reserved.

Références

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Auteurs

Travis J Nelson (TJ)

Department of Chemistry and Nebraska Center for Integrated Biomolecular Communication, University of Nebraska-Lincoln, Lincoln, NE, United States.

Jia Zhao (J)

Department of Chemistry and Nebraska Center for Integrated Biomolecular Communication, University of Nebraska-Lincoln, Lincoln, NE, United States.

Cliff I Stains (CI)

Department of Chemistry and Nebraska Center for Integrated Biomolecular Communication, University of Nebraska-Lincoln, Lincoln, NE, United States; Cancer Genes and Molecular Recognition Program, Fred & Pamela Buffet Cancer Center, University of Nebraska Medical Center, Omaha, NE, United States. Electronic address: cstains2@unl.edu.

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Classifications MeSH