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
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author Bouvier, Denis
Labessan, Natty
Clémancey, Martin
Latour, Jean-Marc
Ravanat, Jean-Luc
Fontecave, Marc
Atta, Mohamed
author_facet Bouvier, Denis
Labessan, Natty
Clémancey, Martin
Latour, Jean-Marc
Ravanat, Jean-Luc
Fontecave, Marc
Atta, Mohamed
author_sort Bouvier, Denis
collection PubMed
description 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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spelling pubmed-40811062014-07-10 TtcA a new tRNA-thioltransferase with an Fe-S cluster Bouvier, Denis Labessan, Natty Clémancey, Martin Latour, Jean-Marc Ravanat, Jean-Luc Fontecave, Marc Atta, Mohamed Nucleic Acids Res Nucleic Acid Enzymes 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. Oxford University Press 2014-08-01 2014-06-26 /pmc/articles/PMC4081106/ /pubmed/24914049 http://dx.doi.org/10.1093/nar/gku508 Text en © The Author(s) 2014. Published by Oxford University Press on behalf of Nucleic Acids Research. http://creativecommons.org/licenses/by-nc/3.0/ This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by-nc/3.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited. For commercial re-use, please contact journals.permissions@oup.com
spellingShingle Nucleic Acid Enzymes
Bouvier, Denis
Labessan, Natty
Clémancey, Martin
Latour, Jean-Marc
Ravanat, Jean-Luc
Fontecave, Marc
Atta, Mohamed
TtcA a new tRNA-thioltransferase with an Fe-S cluster
title TtcA a new tRNA-thioltransferase with an Fe-S cluster
title_full TtcA a new tRNA-thioltransferase with an Fe-S cluster
title_fullStr TtcA a new tRNA-thioltransferase with an Fe-S cluster
title_full_unstemmed TtcA a new tRNA-thioltransferase with an Fe-S cluster
title_short TtcA a new tRNA-thioltransferase with an Fe-S cluster
title_sort ttca a new trna-thioltransferase with an fe-s cluster
topic Nucleic Acid Enzymes
url 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
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