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Jeanmarie Ghuysen - One of the best experts on this subject based on the ideXlab platform.
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the penicillin sensory transducer blar involved in the inducibility of beta lactamase synthesis in bacillus licheniformis is embedded in the plasma membrane via a four alpha helix bundle
Molecular Microbiology, 1997Co-Authors: Karin Hardt, Bernard Joris, Sophie Lepage, Robert Brasseur, Olivier J Lampen, Jeanmarie Frere, Anthony L Fink, Jeanmarie GhuysenAbstract:Prediction studies, conformational analyses and membrane-topology mapping lead to the conclusion that the penicillin sensory transducer, BlaR, involved in the inducibility of β-lactamase synthesis in Bacillus licheniformis, is embedded in the plasma membrane bilayer via four transmembrane segments TM1–TM4 that form a four-α-helix bundle. The extracellular 262-Amino-Acid-Residue polypeptide, S340–R601, that is fused at the carboxy end of TM4, possesses the amino acid sequence signature of a penicilloyl serine transferase. It probably functions as penicillin sensor. As an independent entity, this polypeptide behaves as a high-affinity penicillin-binding protein. As a component of the full-size BlaR, it adopts a different conformation presumably because of interactions with the extracellular 63-Amino-Acid-Residue P53–S115 loop that connects TM2 and TM3. Reception of the penicillin-induced signal requires a precise conformation of the sensor but it does not involve penicilloylation of the serine Residue S402 of motif STYK. Signal transmission through the plasma membrane by the four-α-helix bundle may proceed in a way comparable to that of the aspartate receptor, Tar. Signal emission in the cytosol by the intracellular 189-Amino-Acid-Residue Y134–K322 loop that connects TM3 and TM4, may proceed via the activation of a putative metallopeptidase.
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the penicillin sensory transducer blar involved in the inducibility of beta lactamase synthesis in bacillus licheniformis is embedded in the plasma membrane via a four alpha helix bundle
Molecular Microbiology, 1997Co-Authors: Karin Hardt, Bernard Joris, Sophie Lepage, Robert Brasseur, Olivier J Lampen, Jeanmarie Frere, Anthony L Fink, Jeanmarie GhuysenAbstract:Prediction studies, conformational analyses and membrane-topology mapping lead to the conclusion that the penicillin sensory transducer, BlaR, involved in the inducibility of beta-lactamase synthesis in Bacillus licheniformis, is embedded in the plasma membrane bilayer via four transmembrane segments TM1-TM4 that form a four-alpha-helix bundle. The extracellular 262-Amino-Acid-Residue polypeptide, S340-R601, that is fused at the carboxy end of TM4, possesses the amino acid sequence signature of a penicilloyl serine transferase. It probably functions as penicillin sensor. As an independent entity, this polypeptide behaves as a high-affinity penicillin-binding protein. As a component of the full-size BlaR, it adopts a different conformation presumably because of interactions with the extracellular 63-Amino-Acid-Residue P53-S115 loop that connects TM2 and TM3. Reception of the penicillin-induced signal requires a precise conformation of the sensor but it does not involve penicilloylation of the serine Residue S402 of motif STYK. Signal transmission through the plasma membrane by the four-alpha-helix bundle may proceed in a way comparable to that of the aspartate receptor, Tar. Signal emission in the cytosol by the intracellular 189-Amino-Acid-Residue Y134-K322 loop that connects TM3 and TM4, may proceed via the activation of a putative metallopeptidase.
Karin Hardt - One of the best experts on this subject based on the ideXlab platform.
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the penicillin sensory transducer blar involved in the inducibility of beta lactamase synthesis in bacillus licheniformis is embedded in the plasma membrane via a four alpha helix bundle
Molecular Microbiology, 1997Co-Authors: Karin Hardt, Bernard Joris, Sophie Lepage, Robert Brasseur, Olivier J Lampen, Jeanmarie Frere, Anthony L Fink, Jeanmarie GhuysenAbstract:Prediction studies, conformational analyses and membrane-topology mapping lead to the conclusion that the penicillin sensory transducer, BlaR, involved in the inducibility of β-lactamase synthesis in Bacillus licheniformis, is embedded in the plasma membrane bilayer via four transmembrane segments TM1–TM4 that form a four-α-helix bundle. The extracellular 262-Amino-Acid-Residue polypeptide, S340–R601, that is fused at the carboxy end of TM4, possesses the amino acid sequence signature of a penicilloyl serine transferase. It probably functions as penicillin sensor. As an independent entity, this polypeptide behaves as a high-affinity penicillin-binding protein. As a component of the full-size BlaR, it adopts a different conformation presumably because of interactions with the extracellular 63-Amino-Acid-Residue P53–S115 loop that connects TM2 and TM3. Reception of the penicillin-induced signal requires a precise conformation of the sensor but it does not involve penicilloylation of the serine Residue S402 of motif STYK. Signal transmission through the plasma membrane by the four-α-helix bundle may proceed in a way comparable to that of the aspartate receptor, Tar. Signal emission in the cytosol by the intracellular 189-Amino-Acid-Residue Y134–K322 loop that connects TM3 and TM4, may proceed via the activation of a putative metallopeptidase.
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the penicillin sensory transducer blar involved in the inducibility of beta lactamase synthesis in bacillus licheniformis is embedded in the plasma membrane via a four alpha helix bundle
Molecular Microbiology, 1997Co-Authors: Karin Hardt, Bernard Joris, Sophie Lepage, Robert Brasseur, Olivier J Lampen, Jeanmarie Frere, Anthony L Fink, Jeanmarie GhuysenAbstract:Prediction studies, conformational analyses and membrane-topology mapping lead to the conclusion that the penicillin sensory transducer, BlaR, involved in the inducibility of beta-lactamase synthesis in Bacillus licheniformis, is embedded in the plasma membrane bilayer via four transmembrane segments TM1-TM4 that form a four-alpha-helix bundle. The extracellular 262-Amino-Acid-Residue polypeptide, S340-R601, that is fused at the carboxy end of TM4, possesses the amino acid sequence signature of a penicilloyl serine transferase. It probably functions as penicillin sensor. As an independent entity, this polypeptide behaves as a high-affinity penicillin-binding protein. As a component of the full-size BlaR, it adopts a different conformation presumably because of interactions with the extracellular 63-Amino-Acid-Residue P53-S115 loop that connects TM2 and TM3. Reception of the penicillin-induced signal requires a precise conformation of the sensor but it does not involve penicilloylation of the serine Residue S402 of motif STYK. Signal transmission through the plasma membrane by the four-alpha-helix bundle may proceed in a way comparable to that of the aspartate receptor, Tar. Signal emission in the cytosol by the intracellular 189-Amino-Acid-Residue Y134-K322 loop that connects TM3 and TM4, may proceed via the activation of a putative metallopeptidase.
Ralf Jacob - One of the best experts on this subject based on the ideXlab platform.
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a glutamine to proline exchange at amino acid Residue 1098 in sucrase causes a temperature sensitive arrest of sucrase isomaltase in the endoplasmic reticulum and cis golgi
Journal of Biological Chemistry, 2003Co-Authors: Marcus J Propsting, Ralf JacobAbstract:A striking feature of phenotype II in congenital sucrase-isomaltase deficiency is the retention of the brush border protein sucrase-isomaltase (SI) in the cis-Golgi. This transport block is the consequence of a glutamine to proline substitution at amino acid Residue 1098 of the sucrase subunit. Here we provide unequivocal biochemical and confocal data to show that the SI(Q/P) mutant reveals characteristics of a temperature-sensitive mutant. Thus, correct folding, competent intracellular transport, and full enzymatic activity can be partially restored by expression of the mutant SI(Q/P) at the permissive temperature of 20 degrees C instead of 37 degrees C. The acquisition of normal trafficking and function appears to utilize several cycles of anterograde and retrograde steps between the endoplasmic reticulum and the Golgi implicating the molecular chaperones calnexin and heavy chain-binding protein. The data presented in this communication are to our knowledge the first to implicate a temperature-sensitive mutation in an intestinal enzyme deficiency or an intestinal disorder.
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a glutamine to proline exchange at amino acid Residue 1098 in sucrase causes a temperature sensitive arrest of sucrase isomaltase in the endoplasmic reticulum and cis golgi
Journal of Biological Chemistry, 2003Co-Authors: Marcus J Propsting, Ralf JacobAbstract:Abstract A striking feature of phenotype II in congenital sucrase-isomaltase deficiency is the retention of the brush border protein sucrase-isomaltase (SI) in the cis-Golgi. This transport block is the consequence of a glutamine to proline substitution at amino acid Residue 1098 of the sucrase subunit. Here we provide unequivocal biochemical and confocal data to show that the SIQ/P mutant reveals characteristics of a temperature-sensitive mutant. Thus, correct folding, competent intracellular transport, and full enzymatic activity can be partially restored by expression of the mutant SIQ/P at the permissive temperature of 20 °C instead of 37 °C. The acquisition of normal trafficking and function appears to utilize several cycles of anterograde and retrograde steps between the endoplasmic reticulum and the Golgi implicating the molecular chaperones calnexin and heavy chain-binding protein. The data presented in this communication are to our knowledge the first to implicate a temperature-sensitive mutation in an intestinal enzyme deficiency or an intestinal disorder.
Olivier J Lampen - One of the best experts on this subject based on the ideXlab platform.
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the penicillin sensory transducer blar involved in the inducibility of beta lactamase synthesis in bacillus licheniformis is embedded in the plasma membrane via a four alpha helix bundle
Molecular Microbiology, 1997Co-Authors: Karin Hardt, Bernard Joris, Sophie Lepage, Robert Brasseur, Olivier J Lampen, Jeanmarie Frere, Anthony L Fink, Jeanmarie GhuysenAbstract:Prediction studies, conformational analyses and membrane-topology mapping lead to the conclusion that the penicillin sensory transducer, BlaR, involved in the inducibility of β-lactamase synthesis in Bacillus licheniformis, is embedded in the plasma membrane bilayer via four transmembrane segments TM1–TM4 that form a four-α-helix bundle. The extracellular 262-Amino-Acid-Residue polypeptide, S340–R601, that is fused at the carboxy end of TM4, possesses the amino acid sequence signature of a penicilloyl serine transferase. It probably functions as penicillin sensor. As an independent entity, this polypeptide behaves as a high-affinity penicillin-binding protein. As a component of the full-size BlaR, it adopts a different conformation presumably because of interactions with the extracellular 63-Amino-Acid-Residue P53–S115 loop that connects TM2 and TM3. Reception of the penicillin-induced signal requires a precise conformation of the sensor but it does not involve penicilloylation of the serine Residue S402 of motif STYK. Signal transmission through the plasma membrane by the four-α-helix bundle may proceed in a way comparable to that of the aspartate receptor, Tar. Signal emission in the cytosol by the intracellular 189-Amino-Acid-Residue Y134–K322 loop that connects TM3 and TM4, may proceed via the activation of a putative metallopeptidase.
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the penicillin sensory transducer blar involved in the inducibility of beta lactamase synthesis in bacillus licheniformis is embedded in the plasma membrane via a four alpha helix bundle
Molecular Microbiology, 1997Co-Authors: Karin Hardt, Bernard Joris, Sophie Lepage, Robert Brasseur, Olivier J Lampen, Jeanmarie Frere, Anthony L Fink, Jeanmarie GhuysenAbstract:Prediction studies, conformational analyses and membrane-topology mapping lead to the conclusion that the penicillin sensory transducer, BlaR, involved in the inducibility of beta-lactamase synthesis in Bacillus licheniformis, is embedded in the plasma membrane bilayer via four transmembrane segments TM1-TM4 that form a four-alpha-helix bundle. The extracellular 262-Amino-Acid-Residue polypeptide, S340-R601, that is fused at the carboxy end of TM4, possesses the amino acid sequence signature of a penicilloyl serine transferase. It probably functions as penicillin sensor. As an independent entity, this polypeptide behaves as a high-affinity penicillin-binding protein. As a component of the full-size BlaR, it adopts a different conformation presumably because of interactions with the extracellular 63-Amino-Acid-Residue P53-S115 loop that connects TM2 and TM3. Reception of the penicillin-induced signal requires a precise conformation of the sensor but it does not involve penicilloylation of the serine Residue S402 of motif STYK. Signal transmission through the plasma membrane by the four-alpha-helix bundle may proceed in a way comparable to that of the aspartate receptor, Tar. Signal emission in the cytosol by the intracellular 189-Amino-Acid-Residue Y134-K322 loop that connects TM3 and TM4, may proceed via the activation of a putative metallopeptidase.
Robert Brasseur - One of the best experts on this subject based on the ideXlab platform.
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the penicillin sensory transducer blar involved in the inducibility of beta lactamase synthesis in bacillus licheniformis is embedded in the plasma membrane via a four alpha helix bundle
Molecular Microbiology, 1997Co-Authors: Karin Hardt, Bernard Joris, Sophie Lepage, Robert Brasseur, Olivier J Lampen, Jeanmarie Frere, Anthony L Fink, Jeanmarie GhuysenAbstract:Prediction studies, conformational analyses and membrane-topology mapping lead to the conclusion that the penicillin sensory transducer, BlaR, involved in the inducibility of β-lactamase synthesis in Bacillus licheniformis, is embedded in the plasma membrane bilayer via four transmembrane segments TM1–TM4 that form a four-α-helix bundle. The extracellular 262-Amino-Acid-Residue polypeptide, S340–R601, that is fused at the carboxy end of TM4, possesses the amino acid sequence signature of a penicilloyl serine transferase. It probably functions as penicillin sensor. As an independent entity, this polypeptide behaves as a high-affinity penicillin-binding protein. As a component of the full-size BlaR, it adopts a different conformation presumably because of interactions with the extracellular 63-Amino-Acid-Residue P53–S115 loop that connects TM2 and TM3. Reception of the penicillin-induced signal requires a precise conformation of the sensor but it does not involve penicilloylation of the serine Residue S402 of motif STYK. Signal transmission through the plasma membrane by the four-α-helix bundle may proceed in a way comparable to that of the aspartate receptor, Tar. Signal emission in the cytosol by the intracellular 189-Amino-Acid-Residue Y134–K322 loop that connects TM3 and TM4, may proceed via the activation of a putative metallopeptidase.
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the penicillin sensory transducer blar involved in the inducibility of beta lactamase synthesis in bacillus licheniformis is embedded in the plasma membrane via a four alpha helix bundle
Molecular Microbiology, 1997Co-Authors: Karin Hardt, Bernard Joris, Sophie Lepage, Robert Brasseur, Olivier J Lampen, Jeanmarie Frere, Anthony L Fink, Jeanmarie GhuysenAbstract:Prediction studies, conformational analyses and membrane-topology mapping lead to the conclusion that the penicillin sensory transducer, BlaR, involved in the inducibility of beta-lactamase synthesis in Bacillus licheniformis, is embedded in the plasma membrane bilayer via four transmembrane segments TM1-TM4 that form a four-alpha-helix bundle. The extracellular 262-Amino-Acid-Residue polypeptide, S340-R601, that is fused at the carboxy end of TM4, possesses the amino acid sequence signature of a penicilloyl serine transferase. It probably functions as penicillin sensor. As an independent entity, this polypeptide behaves as a high-affinity penicillin-binding protein. As a component of the full-size BlaR, it adopts a different conformation presumably because of interactions with the extracellular 63-Amino-Acid-Residue P53-S115 loop that connects TM2 and TM3. Reception of the penicillin-induced signal requires a precise conformation of the sensor but it does not involve penicilloylation of the serine Residue S402 of motif STYK. Signal transmission through the plasma membrane by the four-alpha-helix bundle may proceed in a way comparable to that of the aspartate receptor, Tar. Signal emission in the cytosol by the intracellular 189-Amino-Acid-Residue Y134-K322 loop that connects TM3 and TM4, may proceed via the activation of a putative metallopeptidase.