HutT functions as the major L‐histidine transporter in <i>Pseudomonas putida</i> KT2440

Wirtz, Larissa; Eder, Michelle; Brand, Anna-Katharina; Jung, Heinrich

doi:10.1002/1873-3468.14159

Cited by 5 publications

(4 citation statements)

References 54 publications

(100 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Histidine is an important carbon and nitrogen source in Proteobacteria 28 through its conversion to glutamate. The histidine utilization ( hut ) operon involves four enzyme-encoding genes: hutH , hutU , hutI , and hutG ( Figure 5 C).…”

Section: Resultsmentioning

confidence: 99%

Potential therapeutic implications of histidine catabolism by the gut microbiota in NAFLD patients with morbid obesity

Quesada-Vázquez,

Castells-Nobau,

Latorre

et al. 2023

Cell Reports Medicine

View full text Add to dashboard Cite

Section: Resultsmentioning

confidence: 99%

Potential therapeutic implications of histidine catabolism by the gut microbiota in NAFLD patients with morbid obesity

Quesada-Vázquez,

Castells-Nobau,

Latorre

et al. 2023

Cell Reports Medicine

View full text Add to dashboard Cite

“…It is thus tempting to speculate that the genome of B. subtilis encodes one or more low-affinity transporters for histidine. Indeed, B. subtilis encodes several homologs of the Pseudomonas putida histidine transporter HutT (Wirtz et al, 2021). These transporters all belong to the amino acid-polyamine-organocation (APC) superfamily of amino acid transporters.…”

Section: Discussionmentioning

confidence: 99%

How to deal with toxic amino acids: the bipartite AzlCD complex exports histidine in Bacillus subtilis

Meißner

Schramm

Hoßbach

et al. 2022

Preprint

View full text Add to dashboard Cite

In the Gram-positive model bacterium Bacillus subtilis, the presence of the amino acid glutamate triggers potassium uptake due to the glutamate-mediated activation of the potassium channel KtrCD. As a result, the intracellular accumulation of glutamate is toxic in strains lacking the second messenger cyclic di-AMP since these cells are unable to limit potassium uptake. We observed that the presence of histidine, which is degraded to glutamate, is also toxic for a B. subtilis strain that lacks all three c-di-AMP synthesizing enzymes. However, suppressor mutants emerged, and whole genome sequencing revealed mutations in the azlB gene encoding the repressor of the azl operon. This operon encodes an exporter and an importer for branched-chain amino acids. The suppressor mutations result in overexpression of the azl operon. Deletion of the azlCD genes encoding the branched chain amino acid exporter restored the toxicity of histidine indicating that this exporter is required for histidine export and resistance to otherwise toxic levels of the amino acid. The higher abundance of the amino acid exporter AzlCD increased the extracellular concentration of histidine, thus confirming the new function of AzlCD as a histidine exporter. The azl operon encodes transporters for the uptake and export of amino acids. Unexpectedly, AzlB-mediated repression of the operon remains active even in the presence of amino acids suggesting that expression of the azl operon requires mutational activation by inactivation of AzlB.

show abstract

“…For the pvdT amplicon, restriction enzymes Nde I and Xba I were used, respectively. For overproduction and purification of PvdR, the gene was amplified and subsequently cloned into pUCP20‐ANT2‐ hutT [21], yielding plasmid pUCP20‐ANT2‐ pvdR6His . Amplicons were digested using restriction enzymes Nde I and Xho I.…”

Section: Methodsmentioning

confidence: 99%

The ABC transporter family efflux pump PvdRT‐OpmQ of Pseudomonas putida KT2440: purification and initial characterization

et al. 2023

Self Cite

View full text Add to dashboard Cite

Tripartite efflux systems of the ABC-type family transport a variety of substrates and contribute to the antimicrobial resistance of Gram-negative bacteria. PvdRT-OpmQ, a member of this family, is thought to be involved in the secretion of the newly synthesized and recycled siderophore pyoverdine in Pseudomonas species. Here, we purified and characterized the inner membrane component PvdT and the periplasmic adapter protein PvdR of the plant growth-promoting soil bacterium Pseudomonas putida KT2440. We show that PvdT possesses an ATPase activity that is stimulated by the addition of PvdR. In addition, we provide the first biochemical evidence for direct interactions between pyoverdine and PvdRT.

show abstract

HutT functions as the major L‐histidine transporter in Pseudomonas putida KT2440

Cited by 5 publications

References 54 publications

Potential therapeutic implications of histidine catabolism by the gut microbiota in NAFLD patients with morbid obesity

Potential therapeutic implications of histidine catabolism by the gut microbiota in NAFLD patients with morbid obesity

How to deal with toxic amino acids: the bipartite AzlCD complex exports histidine in Bacillus subtilis

The ABC transporter family efflux pump PvdRT‐OpmQ of Pseudomonas putida KT2440: purification and initial characterization

Contact Info

Product

Resources

About