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 Es-cherichia 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 M ¨ ossbauer 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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Chimie

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Nucl. Acids Res.-2014-Bouvier-7960-70.pdf (3.01 Mo)

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Soumis le : jeudi 16 juin 2016-09:42:05

Dernière modification le : jeudi 11 avril 2024-13:08:13

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hal-01332511 , version 1 (16-06-2016)

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HAL Id : hal-01332511 , version 1
DOI : 10.1093/nar/gku508

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Denis Bouvier, Natty Labessan, Martin Clémancey, Jean-Marc Latour, Jean-Luc Ravanat, et al.. TtcA a new tRNA-thioltransferase with an Fe-S cluster. Nucleic Acids Research, 2014, 42 (12), pp.7960-7970. ⟨10.1093/nar/gku508⟩. ⟨hal-01332511⟩

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