Reductive modification of genetically encoded 3-nitrotyrosine sites in alpha synuclein expressed in E.coli.
Cloning, Molecular
Escherichia coli
/ genetics
Escherichia coli Proteins
/ genetics
Gene Expression
Genetic Vectors
/ chemistry
Green Fluorescent Proteins
/ genetics
Humans
Metabolic Networks and Pathways
/ genetics
Oxidation-Reduction
Protein Engineering
/ methods
Recombinant Proteins
/ chemistry
Tyrosine
/ analogs & derivatives
alpha-Synuclein
/ genetics
3-Aminotyrosine
3-Nitrotyrosine
Alpha synuclein
E.coli
Nitration
Journal
Redox biology
ISSN: 2213-2317
Titre abrégé: Redox Biol
Pays: Netherlands
ID NLM: 101605639
Informations de publication
Date de publication:
09 2019
09 2019
Historique:
received:
17
05
2019
revised:
03
06
2019
accepted:
08
06
2019
pubmed:
22
6
2019
medline:
29
2
2020
entrez:
22
6
2019
Statut:
ppublish
Résumé
Tyrosine nitration is a post-translational protein modification relevant to various pathophysiological processes. Chemical nitration procedures have been used to generate and study nitrated proteins, but these methods regularly lead to modifications at other amino acid residues. A novel strategy employs a genetic code modification that allows incorporation of 3-nitrotyrosine (3-NT) during ribosomal protein synthesis to generate a recombinant protein with defined 3-NT-sites, in the absence of other post-translational modifications. This approach was applied to study the generation and stability of the 3-NT moiety in recombinant proteins produced in E.coli. Nitrated alpha-synuclein (ASYN) was selected as exemplary protein, relevant in Parkinson's disease (PD). A procedure was established to obtain pure tyrosine-modified ASYN in mg amounts. However, a rapid (t
Identifiants
pubmed: 31226647
pii: S2213-2317(19)30558-0
doi: 10.1016/j.redox.2019.101251
pmc: PMC6586993
pii:
doi:
Substances chimiques
Escherichia coli Proteins
0
Recombinant Proteins
0
alpha-Synuclein
0
Green Fluorescent Proteins
147336-22-9
3-aminotyrosine
300-34-5
3-nitrotyrosine
3604-79-3
Tyrosine
42HK56048U
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
101251Informations de copyright
Copyright © 2019 The Authors. Published by Elsevier B.V. All rights reserved.
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