A Database of Drosophila Genes & Genomes

FB2008_06, released July 3, 2008
 

Gene Dmau\mariner\T

General Information
SymbolDmau\mariner\TSpeciesD. mauritiana
Namemariner-element transposaseAnnotation symbol
Feature typetransposable_element_geneFlyBase IDFBgn0013835
Created / Updated2006-08-20/2006-08-20
Genomic Location
Chromosome (arm)Recombination map
Cytogenetic mapSequence location
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Automatically generated summary

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The gene mariner-element transposase is referred to in FlyBase by the symbol Dmau\mariner\T (FBgn0013835). It has not been localized to the genome sequence. Its molecular function is described as: magnesium ion binding; protein homodimerization activity. It is involved in the biological process transposition, DNA-mediated. 45 alleles are reported. No phenotypic data is available. It has no annotated transcripts.
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Experimentally Determined Recombination Data
Location
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Right of (cM)
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Gene Order (in direction of increasing cytology)
References
Gene Order (overall orientation not stated)
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Annotated Polypeptides
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GenBank protein
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InterPro domains - A database of protein families, domains, and functional sites
Transposase, type 1 (IPR001888)
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DNA sequence
Protein sequence
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    Please see the FlyBase Gene Expression Report for details of gene expression from the literature.
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        Allele
        Phenotype manifest in
        Allele
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        Allele of Dmau\mariner\TClassMutagenStocksKnown lesion
        hide Alleles Carried on Transgenic Constructs ( 45 )
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        Allele of Dmau\mariner\TClassMutagenStocksKnown lesion
        Dmau\mariner\T+31.hsloss of function0 Yes
        Dmau\mariner\TA102V.hs0 Yes
        Dmau\mariner\TA26T.hs0 Yes
        Dmau\mariner\TA274V.hs0 Yes
        Dmau\mariner\TD284E.hs0 Yes
        Dmau\mariner\TDpse\Hsp83.PC0 Yes
        Dmau\mariner\TE297K.hs0 Yes
        Dmau\mariner\TE297Kantimorph0 Yes
        Dmau\mariner\TE345K.hs0 Yes
        Dmau\mariner\TG201S.hs0 Yes
        Dmau\mariner\TG292R.hs0 Yes
        Dmau\mariner\TG292R0 Yes
        Dmau\mariner\TG325E.hs0 Yes
        Dmau\mariner\THsp26.Sgs30 Yes
        Dmau\mariner\TM110I.hs0 Yes
        Dmau\mariner\TM1K.hs0 Yes
        Dmau\mariner\TM1Kamorph0 Yes
        Dmau\mariner\TMa3110 Yes
        Dmau\mariner\TMa3310 Yes
        Dmau\mariner\TMa3410 Yes
        Dmau\mariner\TMa3510 Yes
        Dmau\mariner\TMos1-pch0 Yes
        Dmau\mariner\TMos10 Yes
        Dmau\mariner\TMos8640 Yes
        Dmau\mariner\TMos8650 Yes
        Dmau\mariner\TMos8660 Yes
        Dmau\mariner\TMos8930 Yes
        Dmau\mariner\TP235L.hs0 Yes
        Dmau\mariner\TP330S.hs0 Yes
        Dmau\mariner\TR12Q.hs0 Yes
        Dmau\mariner\TR132H.hs0 Yes
        Dmau\mariner\TS99N.hs0 Yes
        Dmau\mariner\TSalG0 Yes
        Dmau\mariner\TSalW0 Yes
        Dmau\mariner\TSphW0 Yes
        Dmau\mariner\TT42I.hs0 Yes
        Dmau\mariner\TT42I0 Yes
        Dmau\mariner\TT88M.hs0 Yes
        Dmau\mariner\TW159stop.hs0 Yes
        Dmau\mariner\Ths.PL0 Yes
        Dmau\mariner\TpA2L0 Yes
        Dmau\mariner\Tpch-Mos10 Yes
        Dmau\mariner\Tpch.hs0 Yes
        Dmau\mariner\Tpch0 Yes
        Dmau\mariner\TΔ61.hsloss of function0 Yes
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        Please look at the allele reports for the complete phenotype data
        PCR amplification provided regions of presumed transposase genes from D.mauritiana and 10 other insects representing 6 additional orders. Sequence analysis revealed a diverse array of mariner elements, with multiple subfamilies, indicating vertical inheritance and horizontal transfer.
        Genetic studies of the Mos1 transposase suggest two distinct types of regulatory mechanism: overproduction inhibition, OPI (in which excessive quantities of the wild type transposase significantly reduce overall frequency of excision of a target Dmau\mariner element) and dominant negative complementation, DNC (which is observed in a significant proportion of hypomorphic mutations in the transposase.
        Genetic and biochemical studies have identified a point mutation in the transposase that shows significant dominant-negative complementation when heterozygous with a wild type coding sequence; this finding suggests that the transposase functions as an oligomer. Application of the yeast two hybrid system implies the transposase consists of subunits that interact. Elevated expression of transposase above a certain threshold decreases the frequency of excision of a mariner target element. Therefore overproduction of transposase may serve as one mechanism by which transposition is regulated.
        The Dmau\wpch mosaicism screen efficiently reveals mutations in the Dmau\mariner\T that are defective in the excision reaction of transposition. Site-directed and EMS induced transposase mutations demonstrate that the D,D(34)D domain cannot be replaced with D,D(34)E domain, identify various essential residues in the transposase and indicate that the majority of hypomorphic transposase mutations impair the activity of the wild-type transposase.
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        Dmau\mariner\T allele
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        Produces phenotype in
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        Dmau\mariner transposase seems to distinguish between the 5' and 3' ends of the Dmau\mariner element. Mutations in the 5' inverted repeat are smaller and more frequent than in the 3' terminal repeat, but secondary mutations in elements with a previous 5' lesion tend to have 3' lesions resembling those normally found at the 5' end.
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        The ITR binding domain of Dmau\mariner\T has been localised between amino acids 1 and 141.
        Dmau\mariner\T encodes a transposase which excises Dmau\mariner\T from plasmid DNA in vitro. The transposase recognises the inverted repeats at the end of Dmau\mariner\T in a sequence specific manner via a DNA binding domain located within the N-terminal 120 amino acids. It binds the right hand inverted repeat about five times more strongly than the left. Dmau\mariner\T transposase monomers bind to each other. Mutations along the length of the Dmau\mariner\T transposase protein reduce the monomer interaction, indicating that no single protein-protein interaction domain is involved.
        During Dmau\mariner transposon DNA cleavage by Dmau\mariner\T: the nontransferred strand is cleaved initially; first strand cleavage is not tightly coupled to second strand cleavage and can occur independently of synapsis; and second strand cleavage of mariner does not occur via a hairpin intermediate.
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        InterPro domains - A database of protein families, domains, and functional sites
        Transposase, type 1 (IPR001888)
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        hide Synonyms & Secondary IDs ( 6 )
        Reported As
        Symbol Synonym
        Dmau\mariner\T
         
        Mos1 Transposase
        Name Synonym
        mariner-element transposase
        Secondary FlyBase IDs
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          hide Recent research papers ( 1 )
          Richardson et al., 2006, EMBO J. 25(6): 1324--1334
          Mechanism of Mos1 transposition: insights from structural analysis. [FBrf0190366]
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