Decreased Transport Restores Growth of a Salmonella enterica apbC Mutant on Tricarballylate

Abstract

Mutants of Iron and sulfur are essential to almost all bacteria, and cofactors containing these elements ([Fe-S] clusters) are nearly ubiquitous. Evolution has harnessed the flexible biochemical and biophysical properties of these cofactors for a variety of cellular functions, including enzymatic reactions, electron transfer, DNA metabolism, and environmental sensing (reviewed in references 8 and 27).Three systems for [Fe-S] cluster biosynthesis have been described in bacteria. Work with Azotobacter vinelandii led to the discovery of the nif (nitrogen fixation) (55) and isc (iron-sulfur cluster) (54) [Fe-S] cluster biosynthetic operons. A third system, encoded by the suf (sulfur utilization factor) operon, was discovered in Escherichia coli (47). The genome of Salmonella enterica serovar Typhimurium encodes both the iscSUA-hscAB-fdx-orf3 and sufABCDSE operons (36,47).Both bioinformatics and in vivo genetic approaches have identified several loci outside the isc, suf, and nif operons that impact [Fe-S] cluster metabolism. The apbC, rseC, and apbE loci were discovered in Salmonella enterica by using sensitive genetic screens that exploited phenotypes described for strains lacking isc operon functions (6,7,38,(44)(45)(46). ApbC is a 40-kDa cytoplasmic protein that can bind and rapidly transfer [Fe-S] clusters to a target protein (15) and hydrolyze ATP (16,44). Both of these activities are necessary for in vivo function (16). ApbC is a representative member of an ancient family of [Fe-S] cluster biosynthetic proteins that evolved before the divergence of the Archaea and Eucarya (13). To our knowledge, all organisms that have sequenced genomes and are known to metabolize iron encode a copy of an apbC homologue. In contrast, the functions of the rseC and apbE gene products remain unknown.The erpA, nfuA, cyaY, and ygfZ genes were identified in bacteria by using bioinformatic approaches, and subsequent physiological studies found that these gene products function in 4,35,37,49). The NfuA and ErpA proteins show sequence similarity to the proposed [Fe-S] cluster-trafficking pro-

Lactobacillus paracaseimetabolism of rice bran reveals metabolome associated withSalmonellaTyphimurium growth reduction

“…Tricarballylate was reported to inhibit citric acid cycle enzymes and was reported to have toxic effects on S. enterica when it was accumulated intracellularly at high levels (Boyd et al . ). Past investigations have associated tricarballylate production with the metabolic activity of healthy intestinal and rumen flora (McDevitt and Goldman ; Cook et al .…”

Cetylpyridinium Trichlorostannate: Synthesis, Antimicrobial Properties, and Controlled-Release Properties via Electrical Resistance Tomography

“… 65 Salmonella enterica serovar Typhimurium is a leading cause of salmonellosis worldwide. 66 Streptococcus mutans is a leading cause of dental caries. 67 We individually cultured these bacterial strains with and without CPC, CPC-Sn, and SnCl 2 for 24 h and measured the cultures’ optical densities.…”

The bacterial MrpORP is a novel Mrp/NBP35 protein involved in iron-sulfur biogenesis

“…P-loop NTPases are one of the largest class of proteins with subgroup members involved in a wide variety of essential cellular functions 8 . The Mrp/NBP35 ATP-binding protein subclass comprises proteins present in all three kingdoms of life and mainly involved in Fe-S cluster biogenesis 7–11,15 .…”

“…For instance, Nbp35 and Cfd1 proteins form an heteromeric scaffold complex in yeast and mammalian CIA pathway, whereas mitochondrial Ind1, belonging also to the Mrp/NBP35 ATP-binding protein subclass, serves as Fe-S cluster carrier to mature respiratory Complex I in yeast 9 . Also, in bacteria, the Salmonella enterica ApbC protein has been shown to be required for the maturation of TcuB, an enzyme necessary to use tricarbalyllate as carbon source and it was proposed to exhert a Fe-S cluster carrier role 10,11 .…”