TY  - JOUR
A1  - Ogunkola, Moses Olalekan
A1  - Guiraudie-Capraz, Gaelle
A1  - Féron, François
A1  - Leimkühler, Silke
T1  - The Human Mercaptopyruvate Sulfurtransferase TUM1 Is Involved in Moco Biosynthesis, Cytosolic tRNA Thiolation and Cellular Bioenergetics in Human Embryonic Kidney Cells
T2  - Biomolecules
N2  - Sulfur is an important element that is incorporated into many biomolecules in humans. The incorporation and transfer of sulfur into biomolecules is, however, facilitated by a series of different sulfurtransferases. Among these sulfurtransferases is the human mercaptopyruvate sulfurtransferase (MPST) also designated as tRNA thiouridine modification protein (TUM1). The role of the human TUM1 protein has been suggested in a wide range of physiological processes in the cell among which are but not limited to involvement in Molybdenum cofactor (Moco) biosynthesis, cytosolic tRNA thiolation and generation of H2S as signaling molecule both in mitochondria and the cytosol. Previous interaction studies showed that TUM1 interacts with the L-cysteine desulfurase NFS1 and the Molybdenum cofactor biosynthesis protein 3 (MOCS3). Here, we show the roles of TUM1 in human cells using CRISPR/Cas9 genetically modified Human Embryonic Kidney cells. Here, we show that TUM1 is involved in the sulfur transfer for Molybdenum cofactor synthesis and tRNA thiomodification by spectrophotometric measurement of the activity of sulfite oxidase and liquid chromatography quantification of the level of sulfur-modified tRNA. Further, we show that TUM1 has a role in hydrogen sulfide production and cellular bioenergetics.
KW  - Moco biosynthesis
KW  - sulfite oxidase
KW  - cytosolic tRNA thiolation
KW  - 5-methoxycarbonylmethyl-2-thiouridine
KW  - H2S biosynthesis
KW  - cellular bioenergetics
Y1  - 2023
UR  - https://publishup.uni-potsdam.de/frontdoor/index/index/docId/57959
SN  - 2218-273X
VL  - 13
SP  - 1
EP  - 23
PB  - MDPI
CY  - Basel, Schweiz
ER  -