Expression, purification and characterization of the second DUSP domain of deubiquitinase USP20/VDU2.

Hu, S ; Chen, X ; et al.

In: Protein expression and purification, Jg. 181 (2021-05-01), S. 105836

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Deubiquitinase USP20/VDU2 (VHL-interacting Deubiquitinating Enzyme 2) has been proved to play vital roles in multiple cellular processes by controlling the life-span of substrate proteins including hypoxia-inducible factor HIF1α, β2-adrenergic receptor, and type 2 iodothyronine deiodinase etc. USP20 contains four distinct structural domains, which include the N-terminal zinc-finger ubiquitin binding domain (ZnF-UBP), the catalytic domain (USP domain), and two tandem DUSP domains (DUSP1 and DUSP2). Here in this study, we report the setting up of the production approach for USP20 DUSP2, and the NMR characterization of the produced target protein. With the assistance of GB1 tag and glycerol, both the solubility and stability of USP20 DUSP2 are significantly enhanced. And by using the optimized protein production procedure, monomeric and stable 15 N, 13 C-labeled USP20 DUSP2 sample for NMR data acquisition was obtained. The secondary structural elements of USP20 DUSP2 were then revealed by the analysis of recorded NMR spectra, and USP20 DUSP2 forms an AB3 fold in solution. The production protocol and NMR characterization results reported in this manuscript could be utilized in the extended structural and functional studies of USP20 DUSP2.

Titel:	Expression, purification and characterization of the second DUSP domain of deubiquitinase USP20/VDU2.
Autor/in / Beteiligte Person:	Hu, S ; Chen, X ; Zhu, M ; Hu, H ; Zhou, C ; Shi, L ; Zhang, N
Link:	Zum Volltext
Zeitschrift:	Protein expression and purification, Jg. 181 (2021-05-01), S. 105836
Veröffentlichung:	Orlando, FL : Academic Press ; <i>Original Publication</i>: San Diego : Academic Press, c1990-, 2021
Medientyp:	academicJournal
ISSN:	1096-0279 (electronic)
DOI:	10.1016/j.pep.2021.105836
Schlagwort:	Humans Protein Domains Recombinant Proteins biosynthesis Recombinant Proteins chemistry Recombinant Proteins genetics Recombinant Proteins isolation & purification Zinc Fingers Ubiquitin Thiolesterase biosynthesis Ubiquitin Thiolesterase chemistry Ubiquitin Thiolesterase genetics Ubiquitin Thiolesterase isolation & purification
Sonstiges:	Nachgewiesen in: MEDLINE Sprachen: English Publication Type: Journal Article; Research Support, Non-U.S. Gov't Language: English [Protein Expr Purif] 2021 May; Vol. 181, pp. 105836. <i>Date of Electronic Publication: </i>2021 Jan 30. MeSH Terms: Ubiquitin Thiolesterase* / biosynthesis ; Ubiquitin Thiolesterase* / chemistry ; Ubiquitin Thiolesterase* / genetics ; Ubiquitin Thiolesterase* / isolation & purification ; Humans ; Protein Domains ; Recombinant Proteins / biosynthesis ; Recombinant Proteins / chemistry ; Recombinant Proteins / genetics ; Recombinant Proteins / isolation & purification ; Zinc Fingers Contributed Indexing: Keywords: DUSP domain; Deubiquitinase; NMR; USP20 Substance Nomenclature: 0 (Recombinant Proteins) ; 0 (USP20 protein, human) ; EC 3.4.19.12 (Ubiquitin Thiolesterase) Entry Date(s): Date Created: 20210202 Date Completed: 20211224 Latest Revision: 20211224 Update Code: 20231215

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