TtcA a new tRNA-thioltransferase with an Fe-S cluster

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 clust...

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Detalles Bibliográficos
Autores principales: Bouvier, Denis, Labessan, Natty, Clémancey, Martin, Latour, Jean-Marc, Ravanat, Jean-Luc, Fontecave, Marc, Atta, Mohamed
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Oxford University Press 2014
Materias:
Nucleic Acid Enzymes
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4081106/
https://www.ncbi.nlm.nih.gov/pubmed/24914049
http://dx.doi.org/10.1093/nar/gku508
Descripción
Sumario: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 Mössbauer 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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