期刊
JOURNAL OF BACTERIOLOGY
卷 190, 期 13, 页码 4596-4602出版社
AMER SOC MICROBIOLOGY
DOI: 10.1128/JB.00262-08
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- NIGMS NIH HHS [F32 GM079938, GM47296, GM079938-02, R01 GM047296, GM62203, R01 GM062203] Funding Source: Medline
Mutants of Salmonella enterica lacking apbC have nutritional and biochemical properties indicative of defects in [Fe-S] cluster metabolism. Here we show that apbC is required for S. enterica to use tricarballylate as a carbon and energy source. Tricarballylate catabolism requires three gene products, TcuA, TcuB, and TcuC. Of relevance to this work is the TcuB protein, which has two [4Fe-4S] clusters required for function, making it a logical target for the apbC effect. TcuB activity was 100-fold lower in an apbC mutant than in the isogenic apbC(+) strain. Genetic data show that derepression of the iscRSUA-hscAB-fdx-orj3 operon or overexpression of iscU from a plasmid compensates for the lack of ApbC during growth on tricarballylate. The studies described herein provide evidence that the scaffold protein IscU has a functional overlap with ApbC and that ApbC function is involved in the synthesis of active TcuB.
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