Recombinant protein expression in Sulfolobus islandicus.
Arabinose-inducible expression
Archaea
His-tagged proteins
Homologous protein expression
Sulfolobales
Thermophilic protein
pSeSD
Journal
Methods in enzymology
ISSN: 1557-7988
Titre abrégé: Methods Enzymol
Pays: United States
ID NLM: 0212271
Informations de publication
Date de publication:
2021
2021
Historique:
entrez:
9
11
2021
pubmed:
10
11
2021
medline:
18
3
2022
Statut:
ppublish
Résumé
Since its invention, recombinant protein expression has greatly facilitated our understanding of various cellular processes in different biological systems because theoretically this technique renders any gene to be expressed in a mesophilic host like Escherichia coli, thus allowing functional characterizations of proteins of interest. However, such a practice has only yielded a limited success for proteins encoded in thermophilic archaea since thermophilic proteins are often present in an insoluble form when expressed in E. coli. As a result, it is advantageous to express recombinant proteins of thermophilic archaea in a homologous host, allowing a native form of recombinant protein to be purified and characterized. Here we present a detailed protocol for the homologous expression and purification of proteins in the thermophilic archaeon, Sulfolobus islandicus Rey15A.
Identifiants
pubmed: 34752289
pii: S0076-6879(21)00188-9
doi: 10.1016/bs.mie.2021.05.006
pii:
doi:
Substances chimiques
Recombinant Proteins
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
275-295Informations de copyright
Copyright © 2021 Elsevier Inc. All rights reserved.