TY  - THES
A1  - Dahl, Jan-Ulrik
T1  - Characterization of the role of the sulfur carrier protein TusA for molybdenum cofactor biosynthesis in Escherichia coli
Y1  - 2013
CY  - Potsdam
ER  - 
TY  - JOUR
A1  - Dahl, Jan-Ulrik
A1  - Urban, Alexander
A1  - Bolte, Andrea
A1  - Sriyabhaya, Promjit
A1  - Donahue, Janet L.
A1  - Nimtz, Manfred
A1  - Larson, Timothy J.
A1  - Leimkühler, Silke
T1  - The identification of a novel protein involved in Molybdenum Cofactor Biosynthesis in Escherichia coli
JF  - The journal of biological chemistry
N2  - Background: In Moco biosynthesis, sulfur is transferred from L-cysteine to MPT synthase, catalyzing the conversion of cPMP to MPT.
 Results: The rhodanese-like protein YnjE is a novel protein involved in Moco biosynthesis.
 Conclusion: YnjE enhances the rate of conversion of cPMP to MPT and interacts with MoeB and IscS. S
 ignificance: To understand the mechanism of sulfur transfer and the role of rhodaneses in the cell.
Y1  - 2011
U6  - https://doi.org/10.1074/jbc.M111.282368
SN  - 0021-9258
VL  - 286
IS  - 41
SP  - 35801
EP  - 35812
PB  - American Society for Biochemistry and Molecular Biology
CY  - Bethesda
ER  - 
TY  - JOUR
A1  - Dahl, Jan-Ulrik
A1  - Radon, Christin
A1  - Bühning, Martin
A1  - Nimtz, Manfred
A1  - Leichert, Lars I.
A1  - Denis, Yann
A1  - Jourlin-Castelli, Cecile
A1  - Iobbi-Nivol, Chantal
A1  - Mejean, Vincent
A1  - Leimkühler, Silke
T1  - The Sulfur Carrier Protein TusA Has a Pleiotropic Role in Escherichia
 coli That Also Affects Molybdenum Cofactor Biosynthesis
JF  - JOURNAL OF BIOLOGICAL CHEMISTRY
N2  - The Escherichia coli L-cysteine desulfurase IscS mobilizes sulfur from L-cysteine for the synthesis of several biomolecules such as iron-sulfur (FeS) clusters, molybdopterin, thiamin, lipoic acid, biotin, and the thiolation of tRNAs. The sulfur transfer from IscS to various biomolecules is mediated by different interaction partners (e.g. TusA for thiomodification of tRNAs, IscU for FeS cluster biogenesis, and ThiI for thiamine biosynthesis/tRNA thiolation), which bind at different sites of IscS. Transcriptomic and proteomic studies of a Delta tusA strain showed that the expression of genes of the moaABCDE operon coding for proteins involved in molybdenum cofactor biosynthesis is increased under aerobic and anaerobic conditions. Additionally, under anaerobic conditions the expression of genes encoding hydrogenase 3 and several molybdoenzymes such as nitrate reductase were also increased. On the contrary, the activity of all molydoenzymes analyzed was significantly reduced in the Delta tusA mutant. Characterization of the Delta tusA strain under aerobic conditions showed an overall low molybdopterin content and an accumulation of cyclic pyranopterin monophosphate. Under anaerobic conditions the activity of nitrate reductase was reduced by only 50%, showing that TusA is not essential for molybdenum cofactor biosynthesis. We present a model in which we propose that the direction of sulfur transfer for each sulfur-containing biomolecule is regulated by the availability of the interaction partner of IscS. We propose that in the absence of TusA, more IscS is available for FeS cluster biosynthesis and that the overproduction of FeS clusters leads to a modified expression of several genes.
Y1  - 2013
U6  - https://doi.org/10.1074/jbc.M112.431569
SN  - 0021-9258
VL  - 288
IS  - 8
SP  - 5426
EP  - 5442
PB  - AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
CY  - BETHESDA
ER  -