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Search results 201 to 242 out of 242 for Mnt

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Type Details Score
GXD Expression    
Probe: MGI:2178134
Assay Type: RT-PCR
Annotation Date: 2002-04-29
Strength: Present
Sex: Not Specified
Emaps: EMAPS:1672827
Stage: TS27
Assay Id: MGI:2178270
Age: postnatal newborn
Image: 4
Specimen Label: Mnt x SD7 Lung
Detected: true
Specimen Num: 4
GXD Expression    
Probe: MGI:2178134
Assay Type: RT-PCR
Annotation Date: 2002-04-29
Strength: Present
Sex: Not Specified
Emaps: EMAPS:1684627
Stage: TS27
Assay Id: MGI:2178270
Age: postnatal newborn
Image: 4
Specimen Label: Mnt x SD7 Liver
Detected: true
Specimen Num: 5
GXD Expression    
Probe: MGI:2178134
Assay Type: RT-PCR
Annotation Date: 2002-04-29
Strength: Present
Sex: Not Specified
Emaps: EMAPS:1737327
Stage: TS27
Assay Id: MGI:2178270
Age: postnatal newborn
Image: 4
Specimen Label: Mnt x SD7 Kidney
Detected: true
Specimen Num: 6
GXD Expression    
Probe: MGI:2178134
Assay Type: RT-PCR
Annotation Date: 2002-04-29
Strength: Present
Sex: Not Specified
Emaps: EMAPS:3287427
Stage: TS27
Assay Id: MGI:2178270
Age: postnatal newborn
Image: 4
Specimen Label: Mnt x SD7 Intestine
Detected: true
Specimen Num: 7
GXD Expression    
Probe: MGI:2178134
Assay Type: RT-PCR
Annotation Date: 2002-04-29
Strength: Present
Sex: Not Specified
Emaps: EMAPS:3557727
Stage: TS27
Assay Id: MGI:2178270
Age: postnatal newborn
Image: 4
Specimen Label: Mnt x SD7 Muscle
Detected: true
Specimen Num: 8
Publication
First Author: Burgering MJ
Year: 1994
Journal: Biochemistry
Title: Solution structure of dimeric Mnt repressor (1-76).
Volume: 33
Issue: 50
Pages: 15036-45
Interaction Experiment
Description: Mnt transcriptional repressor is functionally regulated during cell cycle progression.
Heritable Phenotypic Marker
Type: heritable_phenotypic_marker
Organism: mouse, laboratory
Publication
First Author: Cattanach BM
Year: 2000
Journal: Hum Mol Genet
Title: Two imprinted gene mutations: three phenotypes.
Volume: 9
Issue: 15
Pages: 2263-73
Publication
First Author: Patton T
Year: 2023
Journal: Cell Death Dis
Title: RIPK3 controls MAIT cell accumulation during development but not during infection.
Volume: 14
Issue: 2
Pages: 111
Publication
First Author: Anderson TA
Year: 2003
Journal: Biophys Chem
Title: Role of an N(cap) residue in determining the stability and operator-binding affinity of Arc repressor.
Volume: 100
Issue: 1-3
Pages: 341-50
Publication
First Author: Schreiter ER
Year: 2006
Journal: Proc Natl Acad Sci U S A
Title: NikR-operator complex structure and the mechanism of repressor activation by metal ions.
Volume: 103
Issue: 37
Pages: 13676-81
Protein Domain
Type: Homologous_superfamily
Description: This superfamily represents a domain with a ribbon-helix-helix topology consisting of four helices in an open array of two hairpins. This domain is found in Mnt and Arc, two structurally homologous repressors encoded by bacteriophage P22 [, ]. This entry also includes nickel-responsive regulator []and protein CopG [].
Publication
First Author: Pedulla ML
Year: 2003
Journal: J Bacteriol
Title: Corrected sequence of the bacteriophage p22 genome.
Volume: 185
Issue: 4
Pages: 1475-7
Publication
First Author: Sauer RT
Year: 1983
Journal: J Mol Biol
Title: Primary structure of the immI immunity region of bacteriophage P22.
Volume: 168
Issue: 4
Pages: 699-713
Protein Domain
Type: Domain
Description: The Antirepressor protein ant from Salmonella phage P22 prevents the prophage p22 c2 repressor protein from binding to its operators. It also inhibits the action of other prophage repressor proteins, including those of phages lambda and 434. The synthesis of antirepressor is negatively regulated by the protein products of the two other immi genes, mnt and arc [, , ]. This entry represents the N-terminal domain of this protein and similar proteins from tailed bacteriophages (Caudovirales) and bacterial prophages mostly found in Proteobacteria.
Publication
First Author: Sakon J
Year: 1993
Journal: Biochemistry
Title: Molecular structure of kanamycin nucleotidyltransferase determined to 3.0-A resolution.
Volume: 32
Issue: 45
Pages: 11977-84
Publication
First Author: Schildbach JF
Year: 1999
Journal: Proc Natl Acad Sci U S A
Title: Origins of DNA-binding specificity: role of protein contacts with the DNA backbone.
Volume: 96
Issue: 3
Pages: 811-7
Protein Domain
Type: Family
Description: Detailed sequence analysis suggests that members of this family represent the minimal domain of the PolB nucleotidyltransferase superfamily []. The conservation of the nucleotidyltransferase core and particularly the negatively charged metal-chelating residues lead to the prediction that members of this family possess nucleotidyltransferase activity. Their small size, however, leaves very little beyond the core catalytic domain to help in specific substrate recognition as seen in other, larger members of the PolB superfamily []. The conserved region of the MNTs ("minimal"nucleotidyltransferases) includes approximately 90 amino acid residues that correspond to the core domain of kanamycin nucleotidyltransferase []. A structural model of the MNT domain has been proposed [].
Protein Domain
Type: Homologous_superfamily
Description: This superfamily represents domains with a ribbon-helix-helix core topology consisting of four helices in an open array of two hairpins. Such domains are found in several bacterial and phage repressors, including the Escherichia coli methionine repressor (MetJ), which when combined with S-adenosylmethionine (SAM) represses the expression of the methionine regulon and of enzymes involved in SAM synthesis []. Other bacterial and phage repressors containing domains with a similar fold include the bacterial plasmid-encoded repressors CopG (), the bacterial omega transcription repressor [], and the phage repressors Arc []and Mnt []. These repressors are usually obligate dimers, which pair through a single N-terminal strand, and possess a C-terminal helix-turn-helix unit [].
HT Experiment  
Experiment Type: RNA-Seq
Study Type: Baseline
Source: GEO
Publication
First Author: Cairo S
Year: 2001
Journal: Hum Mol Genet
Title: WBSCR14, a gene mapping to the Williams--Beuren syndrome deleted region, is a new member of the Mlx transcription factor network.
Volume: 10
Issue: 6
Pages: 617-27
Publication
First Author: Tang PC
Year: 2022
Journal: Sci Adv
Title: Single-cell RNA sequencing uncovers a neuron-like macrophage subset associated with cancer pain.
Volume: 8
Issue: 40
Pages: eabn5535
Publication
First Author: Gomis-Rüth FX
Year: 1998
Journal: EMBO J
Title: The structure of plasmid-encoded transcriptional repressor CopG unliganded and bound to its operator.
Volume: 17
Issue: 24
Pages: 7404-15
Publication
First Author: Murayama K
Year: 2001
Journal: J Mol Biol
Title: Crystal structure of omega transcriptional repressor encoded by Streptococcus pyogenes plasmid pSM19035 at 1.5 A resolution.
Volume: 314
Issue: 4
Pages: 789-96
Publication
First Author: Vander Byl C
Year: 2000
Journal: J Bacteriol
Title: Sequence of the genome of Salmonella bacteriophage P22.
Volume: 182
Issue: 22
Pages: 6472-81
Publication
First Author: Songailiene I
Year: 2020
Journal: Mol Cell
Title: HEPN-MNT Toxin-Antitoxin System: The HEPN Ribonuclease Is Neutralized by OligoAMPylation.
Volume: 80
Issue: 6
Pages: 955-970.e7
Protein Domain
Type: Homologous_superfamily
Description: This entry describes prokaryotic proteins including tRNA nuclease HepT from Aphanizomenon flos-aquae, the toxic component of a type II toxin-antitoxin (TA) system comprising a minimal nucleotidyltransferase (MNT) and the accompanying HEPN (higher eukaryotes and prokaryotes nucleotide-binding) protein []. HepT dimerises and enables the formation of a deep cleft at the HEPN-domain interface, containing the RX4-6H motif (where X is any amino acid and the residue immediately after the conserved R is typically a polar amino acid), the active site that functions as an RNA-cleaving RNase []. HepT from Aphanizomenon flos-aquae targets a subset of tRNAs and cuts off 4 nt from the 3' end of tRNA acceptor stem, but its toxicity is neutralized by covalent di-AMPylation performed by the MNT antitoxin [].
Publication
First Author: Jia X
Year: 2018
Journal: J Biol Chem
Title: Structure-function analyses reveal the molecular architecture and neutralization mechanism of a bacterial HEPN-MNT toxin-antitoxin system.
Volume: 293
Issue: 18
Pages: 6812-6823
Publication
First Author: Hurlin PJ
Year: 1999
Journal: EMBO J
Title: Mga, a dual-specificity transcription factor that interacts with Max and contains a T-domain DNA-binding motif.
Volume: 18
Issue: 24
Pages: 7019-28
Publication
First Author: Davies K
Year: 2002
Journal: Development
Title: Disruption of mesodermal enhancers for Igf2 in the minute mutant.
Volume: 129
Issue: 7
Pages: 1657-68
Publication
First Author: Hu X
Year: 2016
Journal: J Biol Chem
Title: MitoNEET Deficiency Alleviates Experimental Alcoholic Steatohepatitis in Mice by Stimulating Endocrine Adiponectin-Fgf15 Axis.
Volume: 291
Issue: 43
Pages: 22482-22495
Publication  
First Author: Prochownik EV
Year: 2022
Journal: Cells
Title: Normal and Neoplastic Growth Suppression by the Extended Myc Network.
Volume: 11
Issue: 4
Publication  
First Author: Sun J
Year: 2023
Journal: Front Genet
Title: Effects of Dlx2 overexpression on the genes associated with the maxillary process in the early mouse embryo.
Volume: 14
Pages: 1085263
Publication
First Author: Yao J
Year: 2020
Journal: Nucleic Acids Res
Title: Novel polyadenylylation-dependent neutralization mechanism of the HEPN/MNT toxin/antitoxin system.
Volume: 48
Issue: 19
Pages: 11054-11067
Publication
First Author: Yao J
Year: 2015
Journal: Microb Biotechnol
Title: Identification and characterization of a HEPN-MNT family type II toxin-antitoxin in Shewanella oneidensis.
Volume: 8
Issue: 6
Pages: 961-73
Protein Domain
Type: Family
Description: This family includes the toxic component HepT of a type II toxin-antitoxin (TA) system, which has RNase activity. These proteins contain a HEPN (higher eukaryotes and prokaryotes nucleotide-binding) domain and are neutralized through tri-AMPylation by the cognate antitoxin MntA, containing a MNT (minimal nucleotidyltransferase) domain [, , ]. HepT-MnA form an heterooctamer (at a 2:6 ratio), a rare organisation for this kind of TA systems. HepT dimerises and enables the formation of a deep cleft at the HEPN-domain interface, containing the RX4-6H motif (where X is any amino acid and the residue immediately after the conserved R is typically a polar amino acid) as the active site that functions as an RNA-cleaving RNase. This type II TA system regulates cell motility and confers plasmid stability []. Due to the prevalence of these HEPN/MNT modules in bacteria and archaea, it has been suggested that these TA systems may also play a role in the environmental adaptation to extreme habitats []. This family also includes uncharacterised putative RNases from bacteria and archaea.
Publication
First Author: Aravind L
Year: 2005
Journal: FEMS Microbiol Rev
Title: The many faces of the helix-turn-helix domain: transcription regulation and beyond.
Volume: 29
Issue: 2
Pages: 231-62
Publication
First Author: Weissbach H
Year: 1991
Journal: Mol Microbiol
Title: Regulation of methionine synthesis in Escherichia coli.
Volume: 5
Issue: 7
Pages: 1593-7
Publication
First Author: Aravind L
Year: 1999
Journal: Nucleic Acids Res
Title: DNA polymerase beta-like nucleotidyltransferase superfamily: identification of three new families, classification and evolutionary history.
Volume: 27
Issue: 7
Pages: 1609-18
Publication
First Author: Gerhard DS
Year: 2004
Journal: Genome Res
Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
Volume: 14
Issue: 10B
Pages: 2121-7
Publication
First Author: Church DM
Year: 2009
Journal: PLoS Biol
Title: Lineage-specific biology revealed by a finished genome assembly of the mouse.
Volume: 7
Issue: 5
Pages: e1000112