<i>E. coli</i> MnmA Is an Fe-S Cluster-Independent 2-Thiouridylase
All kingdoms of life have more than 150 different forms of RNA alterations, with tRNA accounting for around 80% of them. These chemical alterations include, among others, methylation, sulfuration, hydroxylation, and acetylation. These changes are necessary for the proper codon recognition and stabil...
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| Language: | English |
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MDPI AG
2024-02-01
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| Series: | Inorganics |
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| Online Access: | https://www.mdpi.com/2304-6740/12/3/67 |
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| author | Moses Ogunkola Lennart Wolff Eric Asare Fenteng Benjamin R. Duffus Silke Leimkühler |
| author_facet | Moses Ogunkola Lennart Wolff Eric Asare Fenteng Benjamin R. Duffus Silke Leimkühler |
| author_sort | Moses Ogunkola |
| collection | DOAJ |
| description | All kingdoms of life have more than 150 different forms of RNA alterations, with tRNA accounting for around 80% of them. These chemical alterations include, among others, methylation, sulfuration, hydroxylation, and acetylation. These changes are necessary for the proper codon recognition and stability of tRNA. In <i>Escherichia coli</i>, sulfur modification at the wobble uridine (34) of lysine, glutamic acid, and glutamine is essential for codon and anticodon binding and prevents frameshifting during translation. Two important proteins that are involved in this thiolation modification are the L-cysteine desulfurase IscS, the initial sulfur donor, and tRNA-specific 2-thiouridylase MnmA, which adenylates and finally transfers the sulfur from IscS to the tRNA. tRNA-specific 2-thiouridylases are iron–sulfur clusters (Fe-S), either dependent or independent depending on the organism. Here, we dissect the controversy of whether the <i>E. coli</i> MnmA protein is an Fe-S cluster-dependent or independent protein. We show that when Fe-S clusters are bound to MnmA, tRNA thiolation is inhibited, making MnmA an Fe-S cluster-independent protein. We further show that 2-thiouridylase only binds to tRNA from its own organism. |
| first_indexed | 2024-04-24T18:10:45Z |
| format | Article |
| id | doaj.art-d9aa81fc72a74020bb5ad280b51da762 |
| institution | Directory Open Access Journal |
| issn | 2304-6740 |
| language | English |
| last_indexed | 2024-04-24T18:10:45Z |
| publishDate | 2024-02-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Inorganics |
| spelling | doaj.art-d9aa81fc72a74020bb5ad280b51da7622024-03-27T13:47:04ZengMDPI AGInorganics2304-67402024-02-011236710.3390/inorganics12030067<i>E. coli</i> MnmA Is an Fe-S Cluster-Independent 2-ThiouridylaseMoses Ogunkola0Lennart Wolff1Eric Asare Fenteng2Benjamin R. Duffus3Silke Leimkühler4Department of Molecular Enzymology, Institute of Biochemistry and Biology, University of Potsdam, Karl-Liebknecht-Str. 24-25, 14476 Potsdam, GermanyDepartment of Molecular Enzymology, Institute of Biochemistry and Biology, University of Potsdam, Karl-Liebknecht-Str. 24-25, 14476 Potsdam, GermanyDepartment of Molecular Enzymology, Institute of Biochemistry and Biology, University of Potsdam, Karl-Liebknecht-Str. 24-25, 14476 Potsdam, GermanyDepartment of Molecular Enzymology, Institute of Biochemistry and Biology, University of Potsdam, Karl-Liebknecht-Str. 24-25, 14476 Potsdam, GermanyDepartment of Molecular Enzymology, Institute of Biochemistry and Biology, University of Potsdam, Karl-Liebknecht-Str. 24-25, 14476 Potsdam, GermanyAll kingdoms of life have more than 150 different forms of RNA alterations, with tRNA accounting for around 80% of them. These chemical alterations include, among others, methylation, sulfuration, hydroxylation, and acetylation. These changes are necessary for the proper codon recognition and stability of tRNA. In <i>Escherichia coli</i>, sulfur modification at the wobble uridine (34) of lysine, glutamic acid, and glutamine is essential for codon and anticodon binding and prevents frameshifting during translation. Two important proteins that are involved in this thiolation modification are the L-cysteine desulfurase IscS, the initial sulfur donor, and tRNA-specific 2-thiouridylase MnmA, which adenylates and finally transfers the sulfur from IscS to the tRNA. tRNA-specific 2-thiouridylases are iron–sulfur clusters (Fe-S), either dependent or independent depending on the organism. Here, we dissect the controversy of whether the <i>E. coli</i> MnmA protein is an Fe-S cluster-dependent or independent protein. We show that when Fe-S clusters are bound to MnmA, tRNA thiolation is inhibited, making MnmA an Fe-S cluster-independent protein. We further show that 2-thiouridylase only binds to tRNA from its own organism.https://www.mdpi.com/2304-6740/12/3/67tRNAthiouridineiron–sulfur cluster |
| spellingShingle | Moses Ogunkola Lennart Wolff Eric Asare Fenteng Benjamin R. Duffus Silke Leimkühler <i>E. coli</i> MnmA Is an Fe-S Cluster-Independent 2-Thiouridylase Inorganics tRNA thiouridine iron–sulfur cluster |
| title | <i>E. coli</i> MnmA Is an Fe-S Cluster-Independent 2-Thiouridylase |
| title_full | <i>E. coli</i> MnmA Is an Fe-S Cluster-Independent 2-Thiouridylase |
| title_fullStr | <i>E. coli</i> MnmA Is an Fe-S Cluster-Independent 2-Thiouridylase |
| title_full_unstemmed | <i>E. coli</i> MnmA Is an Fe-S Cluster-Independent 2-Thiouridylase |
| title_short | <i>E. coli</i> MnmA Is an Fe-S Cluster-Independent 2-Thiouridylase |
| title_sort | i e coli i mnma is an fe s cluster independent 2 thiouridylase |
| topic | tRNA thiouridine iron–sulfur cluster |
| url | https://www.mdpi.com/2304-6740/12/3/67 |
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