期刊
NUCLEIC ACIDS RESEARCH
卷 42, 期 12, 页码 7960-7970出版社
OXFORD UNIV PRESS
DOI: 10.1093/nar/gku508
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资金
- Agence Nationale de la Recherche-Blanc SPORE-PAIR [ANR-2011-BSV5-02001]
- CEA/Grenoble
TtcA catalyzes the post-transcriptional thiolation of cytosine 32 in some tRNAs. The enzyme from Escherichia coli was homologously overexpressed in E. coli. The purified enzyme is a dimer containing an iron-sulfur cluster and displays activity in in vitro assays. The type and properties of the cluster were investigated using a combination of UV-visible absorption, EPR and Mossbauer spectroscopy, as well as by site-directed mutagenesis. These studies demonstrated that the TtcA enzyme contains a redox-active and oxygen-sensitive [4Fe-4S] cluster, chelated by only three cysteine residues and absolutely essential for activity. TtcA is unique tRNA-thiolating enzyme using an iron-sulfur cluster for catalyzing a non-redox reaction.
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