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Search results 401 to 423 out of 423 for Lsr

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Type Details Score
Publication
- | J:262123
     
First Author: Allen Institute for Brain Science
Year: 2004
Journal: Allen Institute
Title: Allen Brain Atlas: mouse riboprobes
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Publication
- | J:144087
     
First Author: Mouse Genome Informatics Scientific Curators
Year: 2009
Journal: Database Download
Title: Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Genome 430 2.0 Array Platform
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Publication
19636340 | -
First Author: Xue T
Year: 2009
Journal: Cell Res
Title: LsrR-binding site recognition and regulatory characteristics in Escherichia coli AI-2 quorum sensing.
Volume: 19
Issue: 11
Pages: 1258-68
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Publication
21454635 | -
First Author: Marques JC
Year: 2011
Journal: J Biol Chem
Title: Processing the interspecies quorum-sensing signal autoinducer-2 (AI-2): characterization of phospho-(S)-4,5-dihydroxy-2,3-pentanedione isomerization by LsrG protein.
Volume: 286
Issue: 20
Pages: 18331-43
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Publication
25225400 | -
First Author: Marques JC
Year: 2014
Journal: Proc Natl Acad Sci U S A
Title: LsrF, a coenzyme A-dependent thiolase, catalyzes the terminal step in processing the quorum sensing signal autoinducer-2.
Volume: 111
Issue: 39
Pages: 14235-40
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Protein Domain
IPR033673 | LsrF
Type: Family
Description: Autoinducers are signal molecules involved in quorum sensing, the process of chemical communication that bacteria use to assess cell population density and synchronize behaviour. The molecule (S)-4,5-dihydroxy-2,3-pentanedione (DPD) is produced by many different species of bacteria and is the precursor of the signal molecule autoinducer-2 (AI-2).A variety of bacterial species have the ability to sequester and process the AI-2 present in their environment, thereby interfering with the cell-cell communication of other bacteria. This process involves the lsr operon, induced by AI-2. This operon consists of a transport system that facilitates uptake of the signal, a kinase that phosphorylates the signal to phospho-DPD (P-DPD), and enzymes that are responsible for processing the phosphorylated signal, thereby terminating induction of the lsr operon [].One of the enzymes responsible for processing the phosphorylated signal is LsrF. LsrF catalyzes the transfer of an acetyl moiety from 3-hydroxy-5-phosphonooxypentane-2,4-dione to CoA to form glycerone phosphate and acetyl-CoA [].
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Protein Domain
IPR033672 | LsrG
Type: Family
Description: Autoinducers are signal molecules involved in quorum sensing, the process of chemical communication that bacteria use to assess cell population density and synchronize behaviour. The molecule (S)-4,5-dihydroxy-2,3-pentanedione (DPD) is produced by many different species of bacteria and is the precursor of the signal molecule autoinducer-2 (AI-2).A variety of bacterial species have the ability to sequester and process the AI-2 present in their environment, thereby interfering with the cell-cell communication of other bacteria. This process involves the lsr operon, induced by AI-2. This operon consists of a transport system that facilitates uptake of the signal, a kinase that phosphorylates the signal to phospho-DPD (P-DPD), and enzymes that are responsible for processing the phosphorylated signal, thereby terminating induction of the lsr operon [].LsrG catalyzes the conversion of (4S)-4-hydroxy-5-phosphonooxypentane-2,3-dione (P-DPD) to 3-hydroxy-5-phosphonooxypentane-2,4-dione (P-HPD) [].
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Publication
14622426 | -
First Author: Taga ME
Year: 2003
Journal: Mol Microbiol
Title: Lsr-mediated transport and processing of AI-2 in Salmonella typhimurium.
Volume: 50
Issue: 4
Pages: 1411-27
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Protein Domain
IPR030281 | LsrA
Type: Family
Description: LsrA is part of the ABC transporter complex LsrABCD that imports autoinducer 2 (AI-2), a protein that functions in interspecies cell-cell communication in bacteria. LsrA is responsible for energy coupling to the transport system [].AI-2 is synthesised via theenzyme LuxS and can induce transcription of the Lsr (LuxS regulated) operon (lsrACDBFGE) [, ]. The first four genes of the operon, lsrACDB, encode components of the ATP-binding cassette transporter, whereas the remaining two are required for the modification of AI-2 following internalisation [].
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Publication
17557827 | -
First Author: Li J
Year: 2007
Journal: J Bacteriol
Title: Quorum sensing in Escherichia coli is signaled by AI-2/LsrR: effects on small RNA and biofilm architecture.
Volume: 189
Issue: 16
Pages: 6011-20
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Protein Domain
IPR033676 | AI-2_kinase
Type: Family
Description: Autoinducers are signal molecules involved in quorum sensing, the process of chemical communication that bacteria use to assess cell population density and synchronize behaviour. The molecule (S)-4,5-dihydroxy-2,3-pentanedione (DPD) is produced by many different species of bacteria and is the precursor of the signal molecule autoinducer-2 (AI-2).A variety of bacterial species have the ability to sequester and process the AI-2 present in their environment, thereby interfering with the cell-cell communication of other bacteria. This process involves the lsr operon, induced by AI-2. This operon consists of a transport system that facilitates uptake of the signal, a kinase that phosphorylates the signal to phospho-DPD (P-DPD), and enzymes that are responsible for processing the phosphorylated signal, thereby terminating induction of the lsr operon [].Autoinducer-2 kinase (also known as LsrK) phosphorylates AI-2. Phosphorylation serves to trap and activate AI-2 within the cell []. Phosphorylated AI-2 (phospho-DPD) binds and inactivates the transcriptional repressor protein LsrR thereby inducing the expression of the lsr operon and potentially other LsrR-regulated, quorum sensing-related genes [, ].
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Publication
17274596 | -
First Author: Xavier KB
Year: 2007
Journal: ACS Chem Biol
Title: Phosphorylation and processing of the quorum-sensing molecule autoinducer-2 in enteric bacteria.
Volume: 2
Issue: 2
Pages: 128-36
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Protein Domain
IPR038109 | DNA_bind_recomb_sf
Type: Homologous_superfamily
Description: The large serine recombinases (LSRs) are DNA-rearranging enzymes that are members of the serine recombinase or resolvase/invertase superfamily. Most resolvases/invertases have a catalytic domain of ~150 residues at their amino terminus, followed by a small, helix-turn-helix (HTH) DNA-binding domain. The LSRs share a similar amino-terminal catalytic domain, but have much larger carboxyl-terminal regions that range in size from ~300 residues to ~550 residues. The C-terminal region of the LSRs is comprised of multiple structural domains and is responsible for coordination of unique LSRs activities. The LSR C-terminal region is composed of two structural domains: a mixed alpha/beta DNA-binding "recombinase domain"linked to an unusual DNA-binding zinc ribbon domain [, ].The DNA-binding recombinase domain is moderately well conserved among the LSRs and consists of a four stranded β-sheet embedded in a core 4-helix bundle [, ].
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Protein Domain
IPR011109 | DNA_bind_recombinase_dom
Type: Domain
Description: The large serine recombinases (LSRs) are DNA-rearranging enzymes that are members of the serine recombinase or resolvase/invertase superfamily. Most resolvases/invertases have a catalytic domain of ~150 residues at their amino terminus, followed by a small, helix-turn-helix (HTH) DNA-binding domain. The LSRs share a similar amino-terminal catalytic domain, but have much larger carboxyl-terminal regions that range in size from ~300 residues to ~550 residues. The C-terminal region of the LSRs is comprised of multiple structural domains and is responsible for coordination of unique LSRs activities. The LSR C-terminal region is composed of two structural domains: a mixed alpha/beta DNA-binding "recombinase domain"linked to an unusual DNA-binding zinc ribbon domain [, ].The DNA-binding recombinase domain is moderately well conserved among the LSRs and consists of a four stranded β-sheet embedded in a core 4-helix bundle [, ].
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Publication
23821671 | -
First Author: Rutherford K
Year: 2013
Journal: Nucleic Acids Res
Title: Attachment site recognition and regulation of directionality by the serine integrases.
Volume: 41
Issue: 17
Pages: 8341-56
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Publication
23980849 | -
First Author: Van Duyne GD
Year: 2013
Journal: Crit Rev Biochem Mol Biol
Title: Large serine recombinase domain structure and attachment site binding.
Volume: 48
Issue: 5
Pages: 476-91
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Publication
18654634 | J:138216
First Author: Dokmanovic-Chouinard M
Year: 2008
Journal: PLoS Genet
Title: Positional cloning of "Lisch-Like", a candidate modifier of susceptibility to type 2 diabetes in mice.
Volume: 4
Issue: 7
Pages: e1000137
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Publication
19188430 | J:151130
First Author: Narvekar P
Year: 2009
Journal: Diabetes
Title: Liver-specific loss of lipolysis-stimulated lipoprotein receptor triggers systemic hyperlipidemia in mice.
Volume: 58
Issue: 5
Pages: 1040-9
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Publication
37359540 | J:346953
 
First Author: Denis-Lagache N
Year: 2023
Journal: Front Immunol
Title: Attempts to evaluate locus suicide recombination and its potential role in B cell negative selection in the mouse.
Volume: 14
Pages: 1155906
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Publication
21447785 | J:182074
First Author: Jun JY
Year: 2011
Journal: Am J Physiol Endocrinol Metab
Title: Spontaneously diabetic Ins2(+/Akita):apoE-deficient mice exhibit exaggerated hypercholesterolemia and atherosclerosis.
Volume: 301
Issue: 1
Pages: E145-54
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Publication
16143658 | J:106725
First Author: Ji Y
Year: 2006
Journal: Am J Physiol Heart Circ Physiol
Title: Targeted inhibition of sarcoplasmic reticulum CaMKII activity results in alterations of Ca2+ homeostasis and cardiac contractility.
Volume: 290
Issue: 2
Pages: H599-606
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Publication
27636884 | J:253187
First Author: Erlendsson AM
Year: 2016
Journal: PLoS One
Title: Repeated Treatments with Ingenol Mebutate Prevents Progression of UV-Induced Photodamage in Hairless Mice.
Volume: 11
Issue: 9
Pages: e0162597
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Publication
11722742 | -
First Author: Taga ME
Year: 2001
Journal: Mol Microbiol
Title: The LuxS-dependent autoinducer AI-2 controls the expression of an ABC transporter that functions in AI-2 uptake in Salmonella typhimurium.
Volume: 42
Issue: 3
Pages: 777-93
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