The functional diversity of the prokaryotic sulfur carrier protein TusA
- Persulfide groups participate in a wide array of biochemical pathways and are chemically very versatile. The TusA protein has been identified as a central element supplying and transferring sulfur as persulfide to a number of important biosynthetic pathways, like molybdenum cofactor biosynthesis or thiomodifications in nucleosides of tRNAs. In recent years, it has furthermore become obvious that this protein is indispensable for the oxidation of sulfur compounds in the cytoplasm. Phylogenetic analyses revealed that different TusA protein variants exists in certain organisms, that have evolved to pursue specific roles in cellular pathways. The specific TusA-like proteins thereby cannot replace each other in their specific roles and are rather specific to one sulfur transfer pathway or shared between two pathways. While certain bacteria like Escherichia coli contain several copies of TusA-like proteins, in other bacteria like Allochromatium vinosum a single copy of TusA is present with an essential role for this organism. Here, we givePersulfide groups participate in a wide array of biochemical pathways and are chemically very versatile. The TusA protein has been identified as a central element supplying and transferring sulfur as persulfide to a number of important biosynthetic pathways, like molybdenum cofactor biosynthesis or thiomodifications in nucleosides of tRNAs. In recent years, it has furthermore become obvious that this protein is indispensable for the oxidation of sulfur compounds in the cytoplasm. Phylogenetic analyses revealed that different TusA protein variants exists in certain organisms, that have evolved to pursue specific roles in cellular pathways. The specific TusA-like proteins thereby cannot replace each other in their specific roles and are rather specific to one sulfur transfer pathway or shared between two pathways. While certain bacteria like Escherichia coli contain several copies of TusA-like proteins, in other bacteria like Allochromatium vinosum a single copy of TusA is present with an essential role for this organism. Here, we give an overview on the multiple roles of the various TusA-like proteins in sulfur transfer pathways in different organisms to shed light on the remaining mysteries of this versatile protein.…
Author details: | Tomohisa Sebastian Tanabe, Silke LeimkühlerORCiDGND, Christiane DahlORCiDGND |
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DOI: | https://doi.org/10.1016/bs.ampbs.2019.07.004 |
ISBN: | 978-0-12-817715-0 |
ISBN: | 978-0-12-817714-3 |
ISSN: | 0065-2911 |
Pubmed ID: | https://pubmed.ncbi.nlm.nih.gov/31655739 |
Title of parent work (English): | Advances in microbial physiology |
Publisher: | Elsevier Acad. Press |
Place of publishing: | Amsterdam |
Editor(s): | RK Poole |
Publication type: | Article |
Language: | English |
Date of first publication: | 2019/08/23 |
Publication year: | 2019 |
Release date: | 2021/04/22 |
Volume: | 75 |
Number of pages: | 45 |
First page: | 233 |
Last Page: | 277 |
Funding institution: | Deutsche ForschungsgemeinschaftGerman Research Foundation (DFG) [Da 351/6-2, Da 351/81, LE1171/11-2, LE1171/15-2] |
Organizational units: | Mathematisch-Naturwissenschaftliche Fakultät / Institut für Biochemie und Biologie |
DDC classification: | 5 Naturwissenschaften und Mathematik / 57 Biowissenschaften; Biologie / 570 Biowissenschaften; Biologie |
Peer review: | Referiert |