Identification and functional analysis of the mitochondrial cysteine synthase TtCsa2 from Tetrahymena thermophila.
Tetrahymena thermophila
cysteine synthase
heavy metal stresses
mitochondria
mutation
Journal
Journal of cellular biochemistry
ISSN: 1097-4644
Titre abrégé: J Cell Biochem
Pays: United States
ID NLM: 8205768
Informations de publication
Date de publication:
12 2021
12 2021
Historique:
revised:
03
08
2021
received:
06
02
2021
accepted:
12
08
2021
pubmed:
25
8
2021
medline:
15
3
2022
entrez:
24
8
2021
Statut:
ppublish
Résumé
Cysteine is a crucial component for all organisms and plays a critical role in the structure, stability, and catalytic functions of many proteins. Tetrahymena has reverse transsulfuration and de novo pathways for cysteine biosynthesis. Cysteine synthase is involved in the de novo cysteine biosynthesis and catalyzes the production of cysteine from O-acetylserine. The novel cysteine synthase TtCSA2 was identified from Tetrahymena thermophila. The TtCSA2 showed high expression levels at the log-phase and the sexual development stage. The TtCsa2 was localized on the outer mitochondrial membrane throughout different developmental stages. However, the truncated N-terminal signal peptide mutant TtCsa2-ΔN23 was localized into the mitochondria. His-TtCsa2 was expressed in Escherichia coli and purified using affinity chromatography. The His-TtCsa2 showed O-acetylserine sulfhydrylase and serine sulfhydrylase activities. Cysteine and glutathione contents decreased in the csa2KD mutant. Furthermore, mutant cells were sensitive to cadmium and copper stresses. This study indicated that the TtCSA2 was involved in the cysteine synthesis in mitochondria and related to heavy metal stresses resistance in Tetrahymena.
Substances chimiques
Mitochondrial Proteins
0
Protozoan Proteins
0
Cysteine Synthase
EC 2.5.1.47
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
1817-1831Informations de copyright
© 2021 Wiley Periodicals LLC.
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