Oligo-(R)-3-hydroxybutyrate modification of sorting signal enables pore formation by Escherichia coli OmpA.

@article{Negoda2010OligoR3hydroxybutyrateMO,
  title={Oligo-(R)-3-hydroxybutyrate modification of sorting signal enables pore formation by Escherichia coli OmpA.},
  author={Alexander Negoda and Elena Negoda and Rosetta N. Reusch},
  journal={Biochimica et biophysica acta},
  year={2010},
  volume={1798 8},
  pages={
          1480-4
        }
}
View on PubMed
doi.org
10 Citations
Background Citations
5
Results Citations
1

10 Citations

Resolving the native conformation of Escherichia coli OmpA
TLDR
The results suggest that the narrow pore is a folding intermediate, and demonstrate the decisive roles of cOHB‐modification, disulfide bond formation and temperature in folding OmpA into its native large‐pore configuration.
Insights into the structure and assembly of Escherichia coli outer membrane protein A
TLDR
A review of studies to date supports the hypothesis that native OmpA is a single‐domain large pore, while a two‐domain narrow‐pore structure is a folding intermediate or minor conformer.
The Role of Short-Chain Conjugated Poly-(R)-3-Hydroxybutyrate (cPHB) in Protein Folding
  • R. Reusch
  • Biology
    International journal of molecular sciences
  • 2013
TLDR
The physical properties of cPHB indicate it plays important roles in the targeting and folding of c PHB-proteins, and its influence on the folding and structure of outer membrane protein A of Escherichia coli is discussed.
Modification of Membrane and Organelle Proteins by Short-chain
TLDR
The folding and the function(s) of cPHB-modified proteins should always be investigated at or above physiological temperatures.
New insights in the formation of polyhydroxyalkanoate granules (carbonosomes) and novel functions of poly(3-hydroxybutyrate).
TLDR
The previous micelle mode of PHB granule formation is replaced by the Scaffold Model in which the PHB synthase initiation complex is bound to the bacterial nucleoid, and data on other forms ofPHB is highlighted.
Biogenesis of Ion Channels
TLDR
Two simple polymers inorganic polyphosphate (PolyP) and poly-(R)-3-hydroxybutyrate (PHB) were available in the primordial environment that could join together to provide the energy for evolving cells.
In silico design of an immunogen against Acinetobacter baumannii based on a novel model for native structure of Outer membrane protein A.
Molecular complementarity between simple, universal molecules and ions limited phenotype space in the precursors of cells
TLDR
The hypothesis that the direct interactions between PHB, PolyP, polyamines and lipids – modulated by calcium – played a central role in solving the fundamental problems faced by early and modern cells is explored.
Physiological Importance of Poly‐(R)‐3‐hydroxybutyrates
TLDR
The low concentrations, lack of unusual atoms or functional groups, and flexible backbones of this complexed PHB, referred to as cPHB, make them invisible to many analytical procedures; whereas other physical properties make them requisite participants in vital physiological processes as well as contributors to the development of certain diseases.
Determination of Polyhydroxybutyrate (PHB) Posttranslational Modifications of Proteins Using Mass Spectrometry

References

SHOWING 1-10 OF 25 REFERENCES
Sorting signal of Escherichia coli OmpA is modified by oligo-(R)-3-hydroxybutyrate.
Refolded Outer Membrane Protein A of Escherichia coliForms Ion Channels with Two Conductance States in Planar Lipid Bilayers*
TLDR
Wild-type and five single tryptophan mutants of urea-denatured OmpA are shown to refold into functional channels in lipid bilayers and provide a new functional assay for the refolding in vitro of the two respective domains of OMPA.
Export and sorting of theEscherichia coli outer membrane protein OmpA
Results of studies, mostly using the outer membrane, 325 residue protein OmpA, are reviewed which concern its translocation across the plasma membrane and incorporation into the outer membrane…
OmpA protein of Escherichia coli outer membrane occurs in open and closed channel forms.
TLDR
Denaturation of open form OmpA and its subsequent renaturation converted it into a nonfunctional or closed form, suggesting that the open and closed forms represent two alternative conformers of this protein.
Folding and Insertion of the Outer Membrane Protein OmpA Is Assisted by the Chaperone Skp and by Lipopolysaccharide*
TLDR
Results describe a first assisted folding pathway of an integral membrane protein on the example of OmpA, which folded spontaneously into lipid bilayers from a complex of periplasmic Skp, lipopolysaccharide, and LPS.
Pore-forming activity of OmpA protein of Escherichia coli.
The influence of amino substitutions within the mature part of an Escherichia coli outer membrane protein (OmpA) on assembly of the polypeptide into its membrane.
Poly(3-hydroxybutyrate) Is Associated with Specific Proteins in the Cytoplasm and Membranes of Escherichia coli*
TLDR
The studies indicate that the majority of cellular PHB (over 80%) is located in cytoplasmic proteins, especially proteins of the ribosomal fraction, which suggests that PHB is a fundamental constituent of cells that may have physiological functions in addition to facilitating ion transmembrane transport or serving as a carbon reserve.
Folding intermediates of a beta-barrel membrane protein. Kinetic evidence for a multi-step membrane insertion mechanism.
TLDR
A simple folding model for beta-barrel membrane proteins is presented, in which folding and membrane insertion are coupled processes which involve at least four kinetically distinguishable steps and both membrane-bound intermediates can be stabilized in fluid lipid bilayers at low temperatures.
Internal deletions in the gene for an Escherichia coli outer membrane protein define an area possibly important for recognition of the outer membrane by this polypeptide.
...
...