Molecular aspects of phosphate transport in Escherichia coli

@article{Rao1990MolecularAO,
  title={Molecular aspects of phosphate transport in Escherichia coli},
  author={N. N. Subrahmanyeswara Rao and Annamaria Torriani},
  journal={Molecular Microbiology},
  year={1990},
  volume={4}
}
Escherichia coli transports inorganic phosphate (Pi) by the low‐affinity transport system, Pit. When the level of the external Pi is lower than 20μM, another transport system, Pst, is induced with a Kt of 0.25μM. An outer‐membrane porin, PhoE, with a Km of about 1μM is also induced. The outer membrane allows the intake of organic phosphates which are degraded to Pi by phosphatases in the periplasm. The Pi‐binding protein will capture the free Pi produced in the periplasm and direct it to the… Expand
The PhoU Protein from Escherichia coli Interacts with PhoR, PstB, and Metals To Form a Phosphate-Signaling Complex at the Membrane
TLDR
Results support the hypothesis that PhoU is involved in the formation of a signaling complex at the cytoplasmic membrane that responds to environmental Pi levels. Expand
Phosphate-dependent regulation of the low- and high-affinity transport systems in the model actinomycete Streptomyces coelicolor.
TLDR
The transcriptional regulation of the SCO4138 and SCO1845 genes of Streptomyces coelicolor and the two putative low-affinity P(i) transporters PitH1 and PitH2 were studied to propose a model for PhoP regulation of this promoter based on the four promoter DNA-PhoP complexes detected by electrophoretic mobility shift assays and footprinting studies. Expand
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Novel in vivo evidence is provided that PstB1 plays a functional role in phosphate uptake in N. punctiforme and it is demonstrated that the genes pstB2,pstB3, and pstb4 show alterations in expression to compensate for the deletion of pst B1. Expand
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The N-terminal amino acid sequence of the immune serum-precipitable PstB protein was determined, and it corresponded to that deduced from the DNA sequence. Expand
Transcription of the pst Operon of Clostridium acetobutylicum Is Dependent on Phosphate Concentration and pH
TLDR
Additional regulatory sites are proposed in the promoter region, integrating two different extracellular signals, namely, depletion of inorganic phosphate and the pH of the environment. Expand
Sequence, biophysical, and structural analyses of the PstS lipoprotein (BB0215) from Borrelia burgdorferi reveal a likely binding component of an ABC‐type phosphate transporter
TLDR
The high‐resolution crystal structure of the protein in the absence of phosphate reveals that the protein's fold is similar to other phosphate‐binding proteins, and residues that are implicated in phosphate binding in other such proteins are conserved in BbPstS. Expand
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TLDR
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Studies of PhoU in Escherichia coli: Metal Binding, Dimerization,Protein/Protein Interactions, and a Signaling Complex Model
TLDR
This work confirms the hypothesis that the PstSCAB complex senses the environmental phosphate and that phosphate signal is passed through PhoU to PhoR and identifies a structural model for interaction. Expand
Porins Are Required for Uptake of Phosphates by Mycobacterium smegmatis
TLDR
It is concluded that the OM of M. smegmatis represents a permeability barrier for phosphates and that Msp porins are the only OM channels for the diffusion of phosphate in M. smackmatis, and that PhoA is not a surface protein, contrary to a previous report. Expand
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