The Experts below are selected from a list of 42885 Experts worldwide ranked by ideXlab platform
Katarzyna J Bandyra - One of the best experts on this subject based on the ideXlab platform.
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a cooperative pnpase hfq rna Carrier Complex facilitates bacterial riboregulation
2021Co-Authors: Tom Dendooven, Dhriti Sinha, Alzbeta Roeselova, Todd Cameron, Nicholas R De Lay, Ben F Luisi, Katarzyna J BandyraAbstract:Polynucleotide phosphorylase (PNPase) is an ancient exoribonuclease conserved in the course of evolution and is found in species as diverse as bacteria and humans. Paradoxically, Escherichia coli PNPase can act not only as an RNA degrading enzyme but also by an unknown mechanism as a chaperone for small regulatory RNAs (sRNAs), with pleiotropic consequences for gene regulation. We present structures of the ternary assembly formed by PNPase, the RNA chaperone Hfq, and sRNA and show that this Complex boosts sRNA stability in vitro. Comparison of structures for PNPase in RNA Carrier and degradation modes reveals how the RNA is rerouted away from the active site through interactions with Hfq and the KH and S1 domains. Together, these data explain how PNPase is repurposed to protect sRNAs from cellular ribonucleases such as RNase E and could aid RNA presentation to facilitate regulatory actions on target genes.
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a cooperative pnpase hfq rna Carrier Complex facilitates bacterial riboregulation
2020Co-Authors: Tom Dendooven, Dhriti Sinha, Alzbeta Roeselova, Todd Cameron, Nicholas R De Lay, Ben F Luisi, Katarzyna J BandyraAbstract:Polynucleotide phosphorylase (PNPase) is an ancient exoribonuclease conserved in the course of evolution, and is found in species ranging from bacteria to humans. Paradoxically, Escherichia coli PNPase can act as a chaperone for small regulatory RNAs (sRNAs),with pleiotropic consequences for gene regulation, but the mechanism of this phenomenon has remained unclear. We present structures of the ternary assembly formed by PNPase, the RNA chaperone Hfq and sRNA, and show that this Complex boosts sRNA stability in vitro. Comparison of the Carrier Complex structure with the structures of PNPase in the apo state and with bound substrate poised for degradation reveals how the RNA is rerouted away from the enzyme active site through interactions with Hfq and the KH and S1 RNA binding domains of PNPase. Together, these data explain how PNPase is repurposed to protect sRNAs from cellular ribonucleases such as RNase E, and could aid RNA presentation to facilitate regulatory actions on target genes.
Jongsang Park - One of the best experts on this subject based on the ideXlab platform.
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lactose poly ethylene glycol grafted poly l lysine as hepatoma cell targeted gene Carrier
1998Co-Authors: Young Hun Choi, Jongsang ParkAbstract:To investigate the delivery of DNA into cells, lactose-poly(ethylene glycol)-grafted poly-l-lysine (Lac-PEG-PLL) polymers were synthesized as polymeric gene Carriers. The new synthetic Carriers, varying the substitution ratio of lactose-poly(ethylene glycol) (lactose-PEG), were characterized by NMR spectroscopy and size-exclusion chromatography. Electrophoretic mobility assay confirmed that the new gene Carrier makes a Complex with plasmid DNA. The attached poly(ethylene glycol) gives better solubility properties to gene/Carrier Complex. Transfection experiments showed that Lac-PEG-PLL efficiently delivers DNA to a hepatoma cell line in vitro; the best efficiency was achieved at a 1:3 weight ratio of DNA to Carrier. As the lactose-PEG substitution content increased up to 30%, the transfection efficiency increased, which demonstrates that the lactose serves as a targeting moiety. No considerable cytotoxicity was observed due to Lac-PEG-PLL or its Complex with DNA within the concentration range for this exp...
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lactose poly ethylene glycol grafted poly l lysine as hepatoma cell targeted gene Carrier
1998Co-Authors: Young Hun Choi, Jongsang ParkAbstract:To investigate the delivery of DNA into cells, lactose-poly(ethylene glycol)-grafted poly-l-lysine (Lac-PEG-PLL) polymers were synthesized as polymeric gene Carriers. The new synthetic Carriers, varying the substitution ratio of lactose-poly(ethylene glycol) (lactose-PEG), were characterized by NMR spectroscopy and size-exclusion chromatography. Electrophoretic mobility assay confirmed that the new gene Carrier makes a Complex with plasmid DNA. The attached poly(ethylene glycol) gives better solubility properties to gene/Carrier Complex. Transfection experiments showed that Lac-PEG-PLL efficiently delivers DNA to a hepatoma cell line in vitro; the best efficiency was achieved at a 1:3 weight ratio of DNA to Carrier. As the lactose-PEG substitution content increased up to 30%, the transfection efficiency increased, which demonstrates that the lactose serves as a targeting moiety. No considerable cytotoxicity was observed due to Lac-PEG-PLL or its Complex with DNA within the concentration range for this exp...
Tom Dendooven - One of the best experts on this subject based on the ideXlab platform.
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a cooperative pnpase hfq rna Carrier Complex facilitates bacterial riboregulation
2021Co-Authors: Tom Dendooven, Dhriti Sinha, Alzbeta Roeselova, Todd Cameron, Nicholas R De Lay, Ben F Luisi, Katarzyna J BandyraAbstract:Polynucleotide phosphorylase (PNPase) is an ancient exoribonuclease conserved in the course of evolution and is found in species as diverse as bacteria and humans. Paradoxically, Escherichia coli PNPase can act not only as an RNA degrading enzyme but also by an unknown mechanism as a chaperone for small regulatory RNAs (sRNAs), with pleiotropic consequences for gene regulation. We present structures of the ternary assembly formed by PNPase, the RNA chaperone Hfq, and sRNA and show that this Complex boosts sRNA stability in vitro. Comparison of structures for PNPase in RNA Carrier and degradation modes reveals how the RNA is rerouted away from the active site through interactions with Hfq and the KH and S1 domains. Together, these data explain how PNPase is repurposed to protect sRNAs from cellular ribonucleases such as RNase E and could aid RNA presentation to facilitate regulatory actions on target genes.
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a cooperative pnpase hfq rna Carrier Complex facilitates bacterial riboregulation
2020Co-Authors: Tom Dendooven, Dhriti Sinha, Alzbeta Roeselova, Todd Cameron, Nicholas R De Lay, Ben F Luisi, Katarzyna J BandyraAbstract:Polynucleotide phosphorylase (PNPase) is an ancient exoribonuclease conserved in the course of evolution, and is found in species ranging from bacteria to humans. Paradoxically, Escherichia coli PNPase can act as a chaperone for small regulatory RNAs (sRNAs),with pleiotropic consequences for gene regulation, but the mechanism of this phenomenon has remained unclear. We present structures of the ternary assembly formed by PNPase, the RNA chaperone Hfq and sRNA, and show that this Complex boosts sRNA stability in vitro. Comparison of the Carrier Complex structure with the structures of PNPase in the apo state and with bound substrate poised for degradation reveals how the RNA is rerouted away from the enzyme active site through interactions with Hfq and the KH and S1 RNA binding domains of PNPase. Together, these data explain how PNPase is repurposed to protect sRNAs from cellular ribonucleases such as RNase E, and could aid RNA presentation to facilitate regulatory actions on target genes.
Young Hun Choi - One of the best experts on this subject based on the ideXlab platform.
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lactose poly ethylene glycol grafted poly l lysine as hepatoma cell targeted gene Carrier
1998Co-Authors: Young Hun Choi, Jongsang ParkAbstract:To investigate the delivery of DNA into cells, lactose-poly(ethylene glycol)-grafted poly-l-lysine (Lac-PEG-PLL) polymers were synthesized as polymeric gene Carriers. The new synthetic Carriers, varying the substitution ratio of lactose-poly(ethylene glycol) (lactose-PEG), were characterized by NMR spectroscopy and size-exclusion chromatography. Electrophoretic mobility assay confirmed that the new gene Carrier makes a Complex with plasmid DNA. The attached poly(ethylene glycol) gives better solubility properties to gene/Carrier Complex. Transfection experiments showed that Lac-PEG-PLL efficiently delivers DNA to a hepatoma cell line in vitro; the best efficiency was achieved at a 1:3 weight ratio of DNA to Carrier. As the lactose-PEG substitution content increased up to 30%, the transfection efficiency increased, which demonstrates that the lactose serves as a targeting moiety. No considerable cytotoxicity was observed due to Lac-PEG-PLL or its Complex with DNA within the concentration range for this exp...
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lactose poly ethylene glycol grafted poly l lysine as hepatoma cell targeted gene Carrier
1998Co-Authors: Young Hun Choi, Jongsang ParkAbstract:To investigate the delivery of DNA into cells, lactose-poly(ethylene glycol)-grafted poly-l-lysine (Lac-PEG-PLL) polymers were synthesized as polymeric gene Carriers. The new synthetic Carriers, varying the substitution ratio of lactose-poly(ethylene glycol) (lactose-PEG), were characterized by NMR spectroscopy and size-exclusion chromatography. Electrophoretic mobility assay confirmed that the new gene Carrier makes a Complex with plasmid DNA. The attached poly(ethylene glycol) gives better solubility properties to gene/Carrier Complex. Transfection experiments showed that Lac-PEG-PLL efficiently delivers DNA to a hepatoma cell line in vitro; the best efficiency was achieved at a 1:3 weight ratio of DNA to Carrier. As the lactose-PEG substitution content increased up to 30%, the transfection efficiency increased, which demonstrates that the lactose serves as a targeting moiety. No considerable cytotoxicity was observed due to Lac-PEG-PLL or its Complex with DNA within the concentration range for this exp...
Dhriti Sinha - One of the best experts on this subject based on the ideXlab platform.
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a cooperative pnpase hfq rna Carrier Complex facilitates bacterial riboregulation
2021Co-Authors: Tom Dendooven, Dhriti Sinha, Alzbeta Roeselova, Todd Cameron, Nicholas R De Lay, Ben F Luisi, Katarzyna J BandyraAbstract:Polynucleotide phosphorylase (PNPase) is an ancient exoribonuclease conserved in the course of evolution and is found in species as diverse as bacteria and humans. Paradoxically, Escherichia coli PNPase can act not only as an RNA degrading enzyme but also by an unknown mechanism as a chaperone for small regulatory RNAs (sRNAs), with pleiotropic consequences for gene regulation. We present structures of the ternary assembly formed by PNPase, the RNA chaperone Hfq, and sRNA and show that this Complex boosts sRNA stability in vitro. Comparison of structures for PNPase in RNA Carrier and degradation modes reveals how the RNA is rerouted away from the active site through interactions with Hfq and the KH and S1 domains. Together, these data explain how PNPase is repurposed to protect sRNAs from cellular ribonucleases such as RNase E and could aid RNA presentation to facilitate regulatory actions on target genes.
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a cooperative pnpase hfq rna Carrier Complex facilitates bacterial riboregulation
2020Co-Authors: Tom Dendooven, Dhriti Sinha, Alzbeta Roeselova, Todd Cameron, Nicholas R De Lay, Ben F Luisi, Katarzyna J BandyraAbstract:Polynucleotide phosphorylase (PNPase) is an ancient exoribonuclease conserved in the course of evolution, and is found in species ranging from bacteria to humans. Paradoxically, Escherichia coli PNPase can act as a chaperone for small regulatory RNAs (sRNAs),with pleiotropic consequences for gene regulation, but the mechanism of this phenomenon has remained unclear. We present structures of the ternary assembly formed by PNPase, the RNA chaperone Hfq and sRNA, and show that this Complex boosts sRNA stability in vitro. Comparison of the Carrier Complex structure with the structures of PNPase in the apo state and with bound substrate poised for degradation reveals how the RNA is rerouted away from the enzyme active site through interactions with Hfq and the KH and S1 RNA binding domains of PNPase. Together, these data explain how PNPase is repurposed to protect sRNAs from cellular ribonucleases such as RNase E, and could aid RNA presentation to facilitate regulatory actions on target genes.