Cloning, characterization and expression analysis of glutathione S-transferase from the Antarctic yeast Rhodotorula mucilaginosa AN5.
Adversity adaptation
Enzymatic traits
Gene expression
Glutathione S-Transferase
Rhodotorula mucilaginosa
Journal
Protein expression and purification
ISSN: 1096-0279
Titre abrégé: Protein Expr Purif
Pays: United States
ID NLM: 9101496
Informations de publication
Date de publication:
03 2020
03 2020
Historique:
received:
29
07
2019
revised:
10
10
2019
accepted:
16
10
2019
pubmed:
2
11
2019
medline:
15
12
2020
entrez:
1
11
2019
Statut:
ppublish
Résumé
The gene for glutathione S-transferase (GST) in Antarctic sea-ice yeast Rhodotorula mucilaginosa AN5 was cloned and expressed in Escherichia coli and named RmGST. Sequence analysis showed that the RmGST gene contained a 843 bp open reading frame, which encoded 280 amino acid residues with a calculated molecular mass of 30.4 kDa and isoelectric point of 5.40. RmGST has the typical C- and N-terminal double domains of glutathione S-transferase. Recombinant RmGST (rRmGST) was expressed in E. coli to produce heterologous protein that had a high specific activity of 60.2 U/mg after purification. The apparent K
Identifiants
pubmed: 31669543
pii: S1046-5928(19)30387-0
doi: 10.1016/j.pep.2019.105518
pii:
doi:
Substances chimiques
Recombinant Proteins
0
Glutathione Transferase
EC 2.5.1.18
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
105518Informations de copyright
Copyright © 2019 Elsevier Inc. All rights reserved.