|  Help  |  About  |  Contact Us

Search our database by keyword

Examples

  • Search this entire website. Enter identifiers, names or keywords for genes, diseases, strains, ontology terms, etc. (e.g. Pax6, Parkinson, ataxia)
  • Use OR to search for either of two terms (e.g. OR mus) or quotation marks to search for phrases (e.g. "dna binding").
  • Boolean search syntax is supported: e.g. Balb* for partial matches or mus AND NOT embryo to exclude a term

Search results 1 to 89 out of 89 for Gatc

0.028s

Categories

Hits by Strain

Hits by Category

Type Details Score
Gene
Type: gene
Organism: Homo sapiens
Gene
Type: gene
Organism: Drosophila melanogaster
Gene
Type: gene
Organism: Rattus norvegicus
Gene
Type: gene
Organism: Danio rerio
Protein Coding Gene
Type: protein_coding_gene
Organism: Mus musculus
Protein Domain
Type: Family
Description: The phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS), a major carbohydrate active-transport system, catalyses the phosphorylation of incoming sugar substrates concomitant with their translocation across the cell membrane.This family represents the IIC component of the PTS galactitol-specific family. Gat family PTS systems typically have 3 components: IIA, IIB and IIC [].
Publication
First Author: Nobelmann B
Year: 1996
Journal: J Bacteriol
Title: Molecular analysis of the gat genes from Escherichia coli and of their roles in galactitol transport and metabolism.
Volume: 178
Issue: 23
Pages: 6790-5
Protein Coding Gene
Type: protein_coding_gene
Organism: Mus caroli
Protein Coding Gene
Type: protein_coding_gene
Organism: Mus musculus
Protein Coding Gene
Type: protein_coding_gene
Organism: Mus musculus
Protein Coding Gene
Type: protein_coding_gene
Organism: Mus musculus
Protein Coding Gene
Type: protein_coding_gene
Organism: Mus musculus
Protein Coding Gene
Type: protein_coding_gene
Organism: Mus musculus
Protein Coding Gene
Type: protein_coding_gene
Organism: Mus musculus
Protein Coding Gene
Type: protein_coding_gene
Organism: Mus musculus
Protein Coding Gene
Type: protein_coding_gene
Organism: Mus musculus
Protein Coding Gene
Type: protein_coding_gene
Organism: Mus musculus
Protein Coding Gene
Type: protein_coding_gene
Organism: Mus musculus
Protein Coding Gene
Type: protein_coding_gene
Organism: Mus musculus
Protein Coding Gene
Type: protein_coding_gene
Organism: Mus musculus
Protein Coding Gene
Type: protein_coding_gene
Organism: Mus musculus
Protein Coding Gene
Type: protein_coding_gene
Organism: Mus musculus
Protein Coding Gene
Type: protein_coding_gene
Organism: Mus musculus
Protein Coding Gene
Type: protein_coding_gene
Organism: Mus musculus
Protein Coding Gene
Type: protein_coding_gene
Organism: Mus pahari
Protein Coding Gene
Type: protein_coding_gene
Organism: Mus spretus
Publication
First Author: Echevarría L
Year: 2014
Journal: Biochem J
Title: Glutamyl-tRNAGln amidotransferase is essential for mammalian mitochondrial translation in vivo.
Volume: 460
Issue: 1
Pages: 91-101
Publication      
First Author: Mouse Genome Informatics and the Wellcome Trust Sanger Institute Mouse Genetics Project (MGP)
Year: 2011
Journal: Database Release
Title: Obtaining and Loading Phenotype Annotations from the Wellcome Trust Sanger Institute (WTSI) Mouse Resources Portal
Publication
First Author: Pagliarini DJ
Year: 2008
Journal: Cell
Title: A mitochondrial protein compendium elucidates complex I disease biology.
Volume: 134
Issue: 1
Pages: 112-23
Publication      
First Author: Mouse Genome Informatics Scientific Curators
Year: 2003
Journal: Database Download
Title: Integrating Computational Gene Models into the Mouse Genome Informatics (MGI) Database
Publication      
First Author: Wellcome Trust Sanger Institute
Year: 2009
Journal: MGI Direct Data Submission
Title: Alleles produced for the KOMP project by the Wellcome Trust Sanger Institute
Publication        
First Author: Mouse Genome Informatics Scientific Curators
Year: 2002
Title: Chromosome assignment of mouse genes using the Mouse Genome Sequencing Consortium (MGSC) assembly and the ENSEMBL Database
Publication
First Author: Kawai J
Year: 2001
Journal: Nature
Title: Functional annotation of a full-length mouse cDNA collection.
Volume: 409
Issue: 6821
Pages: 685-90
Publication
First Author: Skarnes WC
Year: 2011
Journal: Nature
Title: A conditional knockout resource for the genome-wide study of mouse gene function.
Volume: 474
Issue: 7351
Pages: 337-42
Publication
First Author: Okazaki Y
Year: 2002
Journal: Nature
Title: Analysis of the mouse transcriptome based on functional annotation of 60,770 full-length cDNAs.
Volume: 420
Issue: 6915
Pages: 563-73
Publication          
First Author: MGD Nomenclature Committee
Year: 1995
Publication        
First Author: Mouse Genome Informatics Scientific Curators
Year: 2010
Title: Human to Mouse ISO GO annotation transfer
Publication        
First Author: Mouse Genome Informatics Scientific Curators
Year: 2001
Title: Gene Ontology Annotation by the MGI Curatorial Staff
Publication
First Author: Diez-Roux G
Year: 2011
Journal: PLoS Biol
Title: A high-resolution anatomical atlas of the transcriptome in the mouse embryo.
Volume: 9
Issue: 1
Pages: e1000582
Publication      
First Author: MGI Genome Annotation Group and UniGene Staff
Year: 2015
Journal: Database Download
Title: MGI-UniGene Interconnection Effort
Publication
First Author: Gaudet P
Year: 2011
Journal: Brief Bioinform
Title: Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium.
Volume: 12
Issue: 5
Pages: 449-62
Publication        
First Author: Mouse Genome Informatics Scientific Curators
Year: 2000
Title: Gene Ontology Annotation by electronic association of SwissProt Keywords with GO terms
Publication      
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
Publication      
First Author: Mouse Genome Informatics Scientific Curators
Year: 2010
Journal: Database Download
Title: Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Genome U74 Array Platform (A, B, C v2).
Publication      
First Author: Allen Institute for Brain Science
Year: 2004
Journal: Allen Institute
Title: Allen Brain Atlas: mouse riboprobes
Publication        
First Author: Mouse Genome Informatics Scientific Curators
Year: 2002
Title: Mouse Genome Informatics Computational Sequence to Gene Associations
Publication      
First Author: Mouse Genome Informatics
Year: 2010
Journal: Database Release
Title: Protein Ontology Association Load.
Publication      
First Author: Mouse Genome Database and National Center for Biotechnology Information
Year: 2000
Journal: Database Release
Title: Entrez Gene Load
Publication      
First Author: Mouse Genome Informatics Group
Year: 2003
Journal: Database Procedure
Title: Automatic Encodes (AutoE) Reference
Publication        
First Author: Mouse Genome Informatics Scientific Curators
Year: 2005
Title: Obtaining and Loading Genome Assembly Coordinates from Ensembl Annotations
Publication      
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 Gene 1.0 ST Array Platform
Publication      
First Author: Bairoch A
Year: 1999
Journal: Database Release
Title: SWISS-PROT Annotated protein sequence database
Publication      
First Author: Mouse Genome Informatics (MGI) and The National Center for Biotechnology Information (NCBI)
Year: 2010
Journal: Database Download
Title: Consensus CDS project
Publication        
First Author: Mouse Genome Informatics Scientific Curators
Year: 2005
Title: Obtaining and loading genome assembly coordinates from NCBI annotations
Publication
First Author: Chung YS
Year: 2009
Journal: Nucleic Acids Res
Title: Structural insights into the cooperative binding of SeqA to a tandem GATC repeat.
Volume: 37
Issue: 10
Pages: 3143-52
DO Term
GO Term
Protein Domain
Type: Domain
Description: The C-terminal domain binds DNA, binding to hemimethylated GATC sequences at oriC [, ]. The structure of the C-terminal domain consists of seven alpha-helices and three-stranded beta-sheet.The binding of the negative modulator of initiation of replication (SeqA) protein to hemimethylated GATC sequences is important in the negative modulation of chromosomal initiation at oriC, and in the formation of SeqA foci necessary for Escherichia coli chromosome segregation []. SeqA tetramers are able to aggregate or multimerize in a reversible, concentration-dependent manner []. Apart from its function in the control of DNA replication, SeqA may also be a specific transcription factor [].
Protein Domain
Type: Homologous_superfamily
Description: The C-terminal domain binds DNA, binding to hemimethylated GATC sequences at oriC [, ]. The structure of the C-terminal domain consists of seven alpha-helices and three-stranded beta-sheet.The binding of the negative modulator of initiation of replication (SeqA) protein to hemimethylated GATC sequences is important in the negative modulation of chromosomal initiation at oriC, and in the formation of SeqA foci necessary for Escherichia coli chromosome segregation []. SeqA tetramers are able to aggregate or multimerize in a reversible, concentration-dependent manner []. Apart from its function in the control of DNA replication, SeqA may also be a specific transcription factor [].
Publication
First Author: Fujikawa N
Year: 2004
Journal: Nucleic Acids Res
Title: Structural and biochemical analyses of hemimethylated DNA binding by the SeqA protein.
Volume: 32
Issue: 1
Pages: 82-92
Publication
First Author: Guarné A
Year: 2002
Journal: Nat Struct Biol
Title: Insights into negative modulation of E. coli replication initiation from the structure of SeqA-hemimethylated DNA complex.
Volume: 9
Issue: 11
Pages: 839-43
Protein Domain
Type: Family
Description: This entry represents a family related to GatC, the third subunit of an enzyme for completing the charging of tRNA(Gln) by amidating the Glu-tRNA(Gln). The few known archaea that contain a member of this family appear to produce Asn-tRNA(Asn) by an analogous amidotransferase reaction. This protein is proposed to substitute for GatC in the charging of both tRNAs.
Publication
First Author: Lee H
Year: 2001
Journal: J Biol Chem
Title: SeqA protein aggregation is necessary for SeqA function.
Volume: 276
Issue: 37
Pages: 34600-6
Publication
First Author: Slomińska M
Year: 2001
Journal: Mol Microbiol
Title: SeqA, the Escherichia coli origin sequestration protein, is also a specific transcription factor.
Volume: 40
Issue: 6
Pages: 1371-9
Protein Domain
Type: Family
Description: The binding of the negative modulator of initiation of replication (SeqA) protein to hemimethylated GATC sequences is important in the negative modulation of chromosomal initiation at oriC, and in the formation of SeqA foci necessary for Escherichia coli chromosome segregation []. SeqA tetramers are able to aggregate or multimerize in a reversible, concentration-dependent manner []. Apart from its function in the control of DNA replication, SeqA may also be a specific transcription factor [].
Protein Domain
Type: Domain
Description: The binding of SeqA protein to hemimethylated GATC sequences is important in the negative modulation of chromosomal initiation at oriC, and in the formation of SeqA foci necessary for Escherichia coli chromosome segregation []. SeqA tetramers are able to aggregate or multimerise in a reversible, concentration-dependent manner []. Apart from its function in the control of DNA replication, SeqA may also be a specific transcription factor [].This family represents the N-terminal domain of SeqA: a short domain that is reported to mediate the dimerisation of SeqA [].
Publication
First Author: Schweizer-Groyer G
Year: 1999
Journal: J Biol Chem
Title: The glucocorticoid response element II is functionally homologous in rat and human insulin-like growth factor-binding protein-1 promoters.
Volume: 274
Issue: 17
Pages: 11679-86
Publication
First Author: Yang Z
Year: 2003
Journal: Nat Struct Biol
Title: Structure of the bacteriophage T4 DNA adenine methyltransferase.
Volume: 10
Issue: 10
Pages: 849-55
Publication
First Author: Tran PH
Year: 1998
Journal: Structure
Title: Crystal structure of the DpnM DNA adenine methyltransferase from the DpnII restriction system of streptococcus pneumoniae bound to S-adenosylmethionine.
Volume: 6
Issue: 12
Pages: 1563-75
Publication
First Author: Wion D
Year: 2006
Journal: Nat Rev Microbiol
Title: N6-methyl-adenine: an epigenetic signal for DNA-protein interactions.
Volume: 4
Issue: 3
Pages: 183-92
Publication
First Author: Løbner-Olesen A
Year: 2005
Journal: Curr Opin Microbiol
Title: Dam methylation: coordinating cellular processes.
Volume: 8
Issue: 2
Pages: 154-60
Protein Domain
Type: Family
Description: In prokaryotes, the major role of DNA methylation is to protect host DNA against degradation by restriction enzymes. There are 2 major classes of DNA methyltransferase that differ in the nature of the modifications they effect. The members of one class (C-MTases) methylate a ring carbon and form C5-methylcytosine (see ). Members of the second class (N-MTases) methylate exocyclic nitrogens and form either N4-methylcytosine(N4-MTases) or N6-methyladenine (N6-MTases). Both classes of MTase utilise the cofactor S-adenosyl-L-methionine (SAM) as the methyl donor and are active as monomeric enzymes [].N-6 adenine-specific DNA methylases () (A-Mtase) are enzymes that specifically methylate the amino group at the C-6 position of adenines in DNA. They include enzymes are found in bacterial restriction-modification systems, as well as solitary enzymes that do not have a restriction enzyme counterpart [].Proteins in this entry are homologous to Dam methyltransferase () from Escherichia coli which recognises the sequence GATC and methylates the adenine moeity. This protein is not part of a restriction modification system and its activity influences cellular functions such as gene transcription, DNA mismatch repair, initiation of chromosome replication and nucleoid structure []. It is dispensible in E. coli, but has been shown to be required for viability in Yersinia and Vibrio species, virulence in Salmonella, and replication in some bacteriophages. Dam methyltransferase consists of a seven-stranded beta sheet sandwiched between two layers of alpha helices [, ]. The beta sheet contains the catalytic domain, while the target recognition domain is composed of five alpha helices and a beta hairpin. The methyl donor binds to a region of the beta sheet, surrounded by conserved residues, which is next to a narrow surface pocket thought to contain the active site.
Protein Domain
Type: Domain
Description: Type II restriction endonucleases () are components of prokaryotic DNA restriction-modification mechanisms that protect the organism against invading foreign DNA. These site-specific deoxyribonucleases catalyse the endonucleolytic cleavage of DNA to give specific double-stranded fragments with terminal 5'-phosphates. Of the 3000 restriction endonucleases that have been characterised, most are homodimeric or tetrameric enzymes that cleave target DNA at sequence-specific sites close to the recognition site. For homodimeric enzymes, the recognition site is usually a palindromic sequence 4-8 bp in length. Most enzymes require magnesium ions as a cofactor for catalysis. Although they can vary in their mode of recognition, many restriction endonucleases share a similar structural core comprising four beta-strands and one alpha-helix, as well as a similar mechanism of cleavage, suggesting a common ancestral origin []. However, there is still considerable diversity amongst restriction endonucleases [, ]. The target site recognition process triggers large conformational changes of the enzyme and the target DNA, leading to the activation of the catalytic centres. Like other DNA binding proteins, restriction enzymes are capable of non-specific DNA binding as well, which is the prerequisite for efficient target site location by facilitated diffusion. Non-specific binding usually does not involve interactions with the bases but only with the DNA backbone []. There are four classes of restriction endonucleases: types I, II,III and IV. All types of enzymes recognise specific short DNA sequences and carry out the endonucleolytic cleavage of DNA to give specific double-stranded fragments with terminal 5'-phosphates. They differ in their recognition sequence, subunit composition, cleavage position, and cofactor requirements [, ], as summarised below:Type I enzymes () cleave at sites remote from recognition site; require both ATP and S-adenosyl-L-methionine to function; multifunctional protein with both restriction and methylase () activities.Type II enzymes () cleave within or at short specific distances from recognition site; most require magnesium; single function (restriction) enzymes independent of methylase.Type III enzymes () cleave at sites a short distance from recognition site; require ATP (but doesn't hydrolyse it); S-adenosyl-L-methionine stimulates reaction but is not required; exists as part of a complex with a modification methylase methylase ().Type IV enzymes target methylated DNA.This entry is found in type II restriction enzymes such as DpmII (), which recognises the double-stranded unmethylated sequence GATC and cleave before G-1 [], where it encompasess the full length of the protein. It is also found in a number of proteins of unknown function, where it is located adjacent to a DNA adenine-specific methyltransferase domain ().
Protein Domain
Type: Family
Description: Type II restriction endonucleases () are components of prokaryotic DNA restriction-modification mechanisms that protect the organism against invading foreign DNA. These site-specific deoxyribonucleases catalyse the endonucleolytic cleavage of DNA to give specific double-stranded fragments with terminal 5'-phosphates. Of the 3000 restriction endonucleases that have been characterised, most are homodimeric or tetrameric enzymes that cleave target DNA at sequence-specific sites close to the recognition site. For homodimeric enzymes, the recognition site is usually a palindromic sequence 4-8 bp in length. Most enzymes require magnesium ions as a cofactor for catalysis. Although they can vary in their mode of recognition, many restriction endonucleases share a similar structural core comprising four beta-strands and one alpha-helix, as well as a similar mechanism of cleavage, suggesting a common ancestral origin []. However, there is still considerable diversity amongst restriction endonucleases [, ]. The target site recognition process triggers large conformational changes of the enzyme and the target DNA, leading to the activation of the catalytic centres. Like other DNA binding proteins, restriction enzymes are capable of non-specific DNA binding as well, which is the prerequisite for efficient target site location by facilitated diffusion. Non-specific binding usually does not involve interactions with the bases but only with the DNA backbone []. There are four classes of restriction endonucleases: types I, II,III and IV. All types of enzymes recognise specific short DNA sequences and carry out the endonucleolytic cleavage of DNA to give specific double-stranded fragments with terminal 5'-phosphates. They differ in their recognition sequence, subunit composition, cleavage position, and cofactor requirements [, ], as summarised below:Type I enzymes () cleave at sites remote from recognition site; require both ATP and S-adenosyl-L-methionine to function; multifunctional protein with both restriction and methylase () activities.Type II enzymes () cleave within or at short specific distances from recognition site; most require magnesium; single function (restriction) enzymes independent of methylase.Type III enzymes () cleave at sites a short distance from recognition site; require ATP (but doesn't hydrolyse it); S-adenosyl-L-methionine stimulates reaction but is not required; exists as part of a complex with a modification methylase methylase ().Type IV enzymes target methylated DNA.This entry represents type II restriction enzymes such as DpmII (), which recognises the double-stranded unmethylated sequence GATC and cleave before G-1 [].
Publication
First Author: Sekizaki T
Year: 2001
Journal: J Bacteriol
Title: Evidence for horizontal transfer of SsuDAT1I restriction-modification genes to the Streptococcus suis genome.
Volume: 183
Issue: 2
Pages: 500-11
Protein Domain
Type: Homologous_superfamily
Description: Type II restriction endonucleases () are components of prokaryotic DNA restriction-modification mechanisms that protect the organism against invading foreign DNA. These site-specific deoxyribonucleases catalyse the endonucleolytic cleavage of DNA to give specific double-stranded fragments with terminal 5'-phosphates. Of the 3000 restriction endonucleases that have been characterised, most are homodimeric or tetrameric enzymes that cleave target DNA at sequence-specific sites close to the recognition site. For homodimeric enzymes, the recognition site is usually a palindromic sequence 4-8 bp in length. Most enzymes require magnesium ions as a cofactor for catalysis. Although they can vary in their mode of recognition, many restriction endonucleases share a similar structural core comprising four beta-strands and one alpha-helix, as well as a similar mechanism of cleavage, suggesting a common ancestral origin []. However, there is still considerable diversity amongst restriction endonucleases [, ]. The target site recognition process triggers large conformational changes of the enzyme and the target DNA, leading to the activation of the catalytic centres. Like other DNA binding proteins, restriction enzymes are capable of non-specific DNA binding as well, which is the prerequisite for efficient target site location by facilitated diffusion. Non-specific binding usually does not involve interactions with the bases but only with the DNA backbone []. There are four classes of restriction endonucleases: types I, II,III and IV. All types of enzymes recognise specific short DNA sequences and carry out the endonucleolytic cleavage of DNA to give specific double-stranded fragments with terminal 5'-phosphates. They differ in their recognition sequence, subunit composition, cleavage position, and cofactor requirements [, ], as summarised below:Type I enzymes () cleave at sites remote from recognition site; require both ATP and S-adenosyl-L-methionine to function; multifunctional protein with both restriction and methylase () activities.Type II enzymes () cleave within or at short specific distances from recognition site; most require magnesium; single function (restriction) enzymes independent of methylase.Type III enzymes () cleave at sites a short distance from recognition site; require ATP (but doesn't hydrolyse it); S-adenosyl-L-methionine stimulates reaction but is not required; exists as part of a complex with a modification methylase methylase ().Type IV enzymes target methylated DNA.This entry represents restriction endonucleases EcoRV, NaeI, HincII, and Sau3AI, as well as the DNA mismatch repair protein MutH, which are closely related in sequence and structure. EcoRV recognises the DNA sequence GATATC and cleaves after T-1 [], NaeI recognises GCCGCC and cleaves after C-2 [], HincII recognises GTYRAC and cleaves after the pyrimidine Y [], and Sau3AI recognises GATC and cleaves prior to G-1 [].MutH, along with MutS and MutL, is essential for initiation of methyl-directed DNA mismatch repair to correct mistakes made during DNA replication in Escherichia coli. MutH cleaves a newly synthesized and unmethylated daughter strand 5' to the sequence d(GATC) in a hemi-methylated duplex. Activation of MutH requires the recognition of a DNA mismatch by MutS and MutL. With sequence homology to Sau3AI and structural similarity to PvuII endonuclease, MutH shows sequence and structural similarity with PvuII and Sau3AI, indicating a strong relationship with these enzymes through divergent evolution, suggesting that type II restriction endonucleases evolved from a common ancestor [].
Protein Domain
Type: Domain
Description: Type II restriction endonucleases () are components of prokaryotic DNA restriction-modification mechanisms that protect the organism against invading foreign DNA. These site-specific deoxyribonucleases catalyse the endonucleolytic cleavage of DNA to give specific double-stranded fragments with terminal 5'-phosphates. Of the 3000 restriction endonucleases that have been characterised, most are homodimeric or tetrameric enzymes that cleave target DNA at sequence-specific sites close to the recognition site. For homodimeric enzymes, the recognition site is usually a palindromic sequence 4-8 bp in length. Most enzymes require magnesium ions as a cofactor for catalysis. Although they can vary in their mode of recognition, many restriction endonucleases share a similar structural core comprising four beta-strands and one alpha-helix, as well as a similar mechanism of cleavage, suggesting a common ancestral origin []. However, there is still considerable diversity amongst restriction endonucleases [, ]. The target site recognition process triggers large conformational changes of the enzyme and the target DNA, leading to the activation of the catalytic centres. Like other DNA binding proteins, restriction enzymes are capable of non-specific DNA binding as well, which is the prerequisite for efficient target site location by facilitated diffusion. Non-specific binding usually does not involve interactions with the bases but only with the DNA backbone []. There are four classes of restriction endonucleases: types I, II,III and IV. All types of enzymes recognise specific short DNA sequences and carry out the endonucleolytic cleavage of DNA to give specific double-stranded fragments with terminal 5'-phosphates. They differ in their recognition sequence, subunit composition, cleavage position, and cofactor requirements [, ], as summarised below:Type I enzymes () cleave at sites remote from recognition site; require both ATP and S-adenosyl-L-methionine to function; multifunctional protein with both restriction and methylase () activities.Type II enzymes () cleave within or at short specific distances from recognition site; most require magnesium; single function (restriction) enzymes independent of methylase.Type III enzymes () cleave at sites a short distance from recognition site; require ATP (but doesn't hydrolyse it); S-adenosyl-L-methionine stimulates reaction but is not required; exists as part of a complex with a modification methylase methylase ().Type IV enzymes target methylated DNA.This entry represents restriction endonucleases EcoRV, NaeI, HincII, and Sau3AI, as well as the DNA mismatch repair protein MutH, which are closely related in sequence and structure. EcoRV recognises the DNA sequence GATATC and cleaves after T-1 [], NaeI recognises GCCGCC and cleaves after C-2 [], HincII recognises GTYRAC and cleaves after the pyrimidine Y [], and Sau3AI recognises GATC and cleaves prior to G-1 [].MutH, along with MutS and MutL, is essential for initiation of methyl-directed DNA mismatch repair to correct mistakes made during DNA replication in Escherichia coli. MutH cleaves a newly synthesized and unmethylated daughter strand 5' to the sequence d(GATC) in a hemi-methylated duplex. Activation of MutH requires the recognition of a DNA mismatch by MutS and MutL. With sequence homology to Sau3AI and structural similarity to PvuII endonuclease, MutH shows sequence and structural similarity with PvuII and Sau3AI, indicating a strong relationship with these enzymes through divergent evolution, suggesting that type II restriction endonucleases evolved from a common ancestor [].
Publication
First Author: Ban C
Year: 1998
Journal: EMBO J
Title: Structural basis for MutH activation in E.coli mismatch repair and relationship of MutH to restriction endonucleases.
Volume: 17
Issue: 5
Pages: 1526-34
Publication
First Author: Friedhoff P
Year: 2001
Journal: J Biol Chem
Title: Sau3AI, a monomeric type II restriction endonuclease that dimerizes on the DNA and thereby induces DNA loops.
Volume: 276
Issue: 26
Pages: 23581-8
Publication
First Author: Huai Q
Year: 2000
Journal: EMBO J
Title: Crystal structure of NaeI-an evolutionary bridge between DNA endonuclease and topoisomerase.
Volume: 19
Issue: 12
Pages: 3110-8
Publication
First Author: Horton NC
Year: 2004
Journal: Biochemistry
Title: DNA cleavage by EcoRV endonuclease: two metal ions in three metal ion binding sites.
Volume: 43
Issue: 22
Pages: 6841-57
Publication
First Author: Etzkorn C
Year: 2004
Journal: J Mol Biol
Title: Mechanistic insights from the structures of HincII bound to cognate DNA cleaved from addition of Mg2+ and Mn2+.
Volume: 343
Issue: 4
Pages: 833-49
Publication  
First Author: Cheng X
Year: 1995
Journal: Annu Rev Biophys Biomol Struct
Title: Structure and function of DNA methyltransferases.
Volume: 24
Pages: 293-318
Publication
First Author: Sistla S
Year: 2004
Journal: Crit Rev Biochem Mol Biol
Title: S-Adenosyl-L-methionine-dependent restriction enzymes.
Volume: 39
Issue: 1
Pages: 1-19
Publication
First Author: Williams RJ
Year: 2003
Journal: Mol Biotechnol
Title: Restriction endonucleases: classification, properties, and applications.
Volume: 23
Issue: 3
Pages: 225-43
Publication
First Author: Pingoud A
Year: 2005
Journal: Cell Mol Life Sci
Title: Type II restriction endonucleases: structure and mechanism.
Volume: 62
Issue: 6
Pages: 685-707
Publication
First Author: Mucke M
Year: 2003
Journal: Nucleic Acids Res
Title: Diversity of type II restriction endonucleases that require two DNA recognition sites.
Volume: 31
Issue: 21
Pages: 6079-84
Publication
First Author: Pingoud V
Year: 2002
Journal: J Biol Chem
Title: Evolutionary relationship between different subgroups of restriction endonucleases.
Volume: 277
Issue: 16
Pages: 14306-14
Publication
First Author: Pingoud A
Year: 2001
Journal: Nucleic Acids Res
Title: Structure and function of type II restriction endonucleases.
Volume: 29
Issue: 18
Pages: 3705-27