Kozaki T

References (9)

Title : Frequencies and evolution of organophosphate insensitive acetylcholinesterase alleles in laboratory and field populations of the house fly, Musca domestica L. - Kozaki_2009_Pestic.Biochem.Physiol_95_6
Author(s) : Kozaki T , Brady SG , Scott JG
Ref : Pesticide Biochemistry and Physiology , 95 :6 , 2009
Abstract : Resistance to organophosphate (OP) and/or carbamate insecticides can be due to mutations in the acetylcholinesterase gene (Ace). Genotypes of house fly, Musca domestica L., Ace were determined in twelve laboratory maintained strains (originally from North America, Europe and Asia) and two field collected populations from New York and Florida. There were 15 Ace alleles found and 11 of the alleles coded for a susceptible form of the enzyme (i.e., V260, A316, G342 and F407). Three of the four resistance alleles were previously described, while one is new. Phylogenetic analysis of the alleles suggests multiple origins of the F407Y mutation and multiple origins of the G342A mutation that confer OP resistance. Genotyping of field collected house flies from New York and Florida populations revealed the presence of only one resistance allele, Acev10 (containing the non-synonymous mutations for A342 and Y407). All other alleles detected from the field-collected flies coded for a susceptible AChE. Thus, we were able to categorize individual flies as having homozygous susceptible (AceS/AceS), homozygous insensitive (AceI/AceI or Acev10/Acev10) or heterozygous AChE. The frequencies of AceS and AceI were not different between the NY2002 and FL2002 populations. Both populations were out of Castle-Hardy-Weinberg equilibrium, having an excess of AceS/AceI individuals and very few AceS/AceS individuals. Comparison of Ace, Vssc and CYP6D1 genotypes indicates individual house flies commonly have resistance alleles at multiple loci. Comparison of genotype data with bioassays, as well as the use of genotype data in resistance studies is discussed.
ESTHER : Kozaki_2009_Pestic.Biochem.Physiol_95_6
PubMedSearch : Kozaki_2009_Pestic.Biochem.Physiol_95_6
PubMedID:
Gene_locus related to this paper: musdo-ACHE

Title : The genome of a lepidopteran model insect, the silkworm Bombyx mori - Xia_2008_Insect.Biochem.Mol.Biol_38_1036
Author(s) : Xia Q , Wang J , Zhou Z , Li R , Fan W , Cheng D , Cheng T , Qin J , Duana J , Xu H , Li Q , Li N , Wang M , Dai F , Liu C , Lin Y , Zhao P , Zhang H , Liu S , Zha X , Li C , Zhao A , Pan M , Pan G , Shen Y , Gao Z , Wang Z , Wang G , Wu Z , Hou Y , Chai C , Yu Q , He N , Zhang Z , Li S , Yang H , Lu C , Xiang Z , Mita K , Kasahara M , Nakatani Y , Yamamoto K , Abe H , Ahsan B , Daimoni T , Doi K , Fujii T , Fujiwara H , Fujiyama A , Futahashi R , Hashimotol S , Ishibashi J , Iwami M , Kadono-Okuda K , Kanamori H , Kataoka H , Katsuma S , Kawaoka S , Kawasaki H , Kohara Y , Kozaki T , Kuroshu RM , Kuwazaki S , Matsushima K , Minami H , Nagayasu Y , Nakagawa T , Narukawa J , Nohata J , Ohishi K , Ono Y , Osanai-Futahashi M , Ozaki K , Qu W , Roller L , Sasaki S , Sasaki T , Seino A , Shimomura M , Shin-I T , Shinoda T , Shiotsuki T , Suetsugu Y , Sugano S , Suwa M , Suzuki Y , Takiya S , Tamura T , Tanaka H , Tanaka Y , Touhara K , Yamada T , Yamakawa M , Yamanaka N , Yoshikawa H , Zhong YS , Shimada T , Morishita S
Ref : Insect Biochemistry & Molecular Biology , 38 :1036 , 2008
Abstract : Bombyx mori, the domesticated silkworm, is a major insect model for research, and the first lepidopteran for which draft genome sequences became available in 2004. Two independent data sets from whole-genome shotgun sequencing were merged and assembled together with newly obtained fosmid- and BAC-end sequences. The remarkably improved new assembly is presented here. The 8.5-fold sequence coverage of an estimated 432 Mb genome was assembled into scaffolds with an N50 size of approximately 3.7 Mb; the largest scaffold was 14.5 million base pairs. With help of a high-density SNP linkage map, we anchored 87% of the scaffold sequences to all 28 chromosomes. A particular feature was the high repetitive sequence content estimated to be 43.6% and that consisted mainly of transposable elements. We predicted 14,623 gene models based on a GLEAN-based algorithm, a more accurate prediction than the previous gene models for this species. Over three thousand silkworm genes have no homologs in other insect or vertebrate genomes. Some insights into gene evolution and into characteristic biological processes are presented here and in other papers in this issue. The massive silk production correlates with the existence of specific tRNA clusters, and of several sericin genes assembled in a cluster. The silkworm's adaptation to feeding on mulberry leaves, which contain toxic alkaloids, is likely linked to the presence of new-type sucrase genes, apparently acquired from bacteria. The silkworm genome also revealed the cascade of genes involved in the juvenile hormone biosynthesis pathway, and a large number of cuticular protein genes.
ESTHER : Xia_2008_Insect.Biochem.Mol.Biol_38_1036
PubMedSearch : Xia_2008_Insect.Biochem.Mol.Biol_38_1036
PubMedID: 19121390
Gene_locus related to this paper: bommo-a0mnw6 , bommo-a1yw85 , bommo-a9ls22 , bommo-ACHE1 , bommo-ACHE2 , bommo-b0fgv8 , bommo-b1q137 , bommo-b1q139 , bommo-b1q140 , bommo-b1q141 , bommo-b2zdz0 , bommo-b3gef6 , bommo-b3gef7 , bommo-b3gs55 , bommo-b3gs56 , bommo-d2ktu3 , bommo-d2ktu5 , bommo-d9ile0 , bommo-e1cga5 , bommo-e1cga6 , bommo-g8fpz6 , bommo-h9iu43 , bommo-h9iu46 , bommo-h9iu47.1 , bommo-h9iu47.2 , bommo-h9iue5 , bommo-h9ivg2 , bommo-h9iwj7 , bommo-h9iwj8 , bommo-h9ix58 , bommo-h9ixi1.1 , bommo-h9ixi1.2 , bommo-h9iy47 , bommo-h9izw1 , bommo-h9j0s4 , bommo-h9j1y0 , bommo-h9j3r0 , bommo-h9j3w6 , bommo-h9j3w7 , bommo-h9j5t0 , bommo-h9j8g3 , bommo-h9j9k9 , bommo-h9j066 , bommo-h9j067 , bommo-h9j593 , bommo-h9j594 , bommo-h9j990 , bommo-h9jde8 , bommo-h9jde9 , bommo-h9jdf0 , bommo-h9jds4 , bommo-h9jle7 , bommo-h9jn83 , bommo-h9jn85 , bommo-h9jrg2 , bommo-h9jyh9 , bommo-JHE , bommo-m1rmh6 , bommo-q1hq05 , bommo-q4tte1 , bommo-h9j592 , bommo-h9j604 , bommo-h9jpm8 , bommo-h9iss4 , bommo-h9j2c7

Title : Comparison of two acetylcholinesterase gene cDNAs of the lesser mealworm, Alphitobius diaperinus, in insecticide susceptible and resistant strains - Kozaki_2008_Arch.Insect.Biochem.Physiol_67_130
Author(s) : Kozaki T , Kimmelblatt BA , Hamm RL , Scott JG
Ref : Archives of Insect Biochemistry & Physiology , 67 :130 , 2008
Abstract : Two cDNAs encoding different acetylcholinesterase (AChE) genes (AdAce1 and AdAce2) were sequenced and analyzed from the lesser mealworm, Alphitobius diaperinus. Both AdAce1 and AdAce2 were highly similar (95 and 93% amino acid identity, respectively) with the Ace genes of Tribolium castaneum. Both AdAce1 and AdAce2 have the conserved residues characteristic of AChE (catalytic triad, intra-disulfide bonds, and so on). Partial cDNA sequences of the Alphitobius Ace genes were compared between two tetrachlorvinphos resistant (Kennebec and Waycross) and one susceptible strain of beetles. Several single nucleotide polymorphisms (SNPs) were detected, but only one non-synonymous mutation was found (A271S in AdAce2). No SNPs were exclusively found in the resistant strains, the A271S mutation does not correspond to any mutations previously reported to alter sensitivity of AChE to organophosphates or carbamates, and the A271S was found only as a heterozygote in one individual from one of the resistant A. diaperinus strains. This suggests that tetrachlorvinphos resistance in the Kennebec and Waycross strains of A. diaperinus is not due to mutations in either AChE gene. The sequences of AdAce1 and AdAce2 provide new information about the evolution of these important genes in insects.
ESTHER : Kozaki_2008_Arch.Insect.Biochem.Physiol_67_130
PubMedSearch : Kozaki_2008_Arch.Insect.Biochem.Physiol_67_130
PubMedID: 18163527
Gene_locus related to this paper: alpdi-ACHE1 , alpdi-ACHE2

Title : Expression of Ace-paralogous acetylcholinesterase of Culex tritaeniorhynchus with an amino acid substitution conferring insecticide insensitivity in baculovirus-insect cell system - 0h_2006_Pestic.Biochem.Physiol_85_46
Author(s) : Oh SH , Kozaki T , Mizuno H , Tomita T , Kono Y
Ref : Pesticide Biochemistry and Physiology , 85 :46 , 2006
Abstract : In Ace paralogous acetylcholinesterase (AP-AChE) of Culex tritaeniorhynchus, an amino acid substitution, Phe455Trp, is accompanied by the insecticide insensitivity. To confirm the responsibility of the substitution to the insensitivity, AP-AChE cDNA with and without a Phe455Trp substitution and Ace orthologous AChE (AO-AChE) cDNA were expressed in a baculovirus-insect cell system and the biochemical properties of AChEs (AP-CxTI, AP-CxTS, and AO-CxT, respectively) determined. AP-CxTI which has the same level of affinity to ACh, the natural substrate, showed a drastic decline in affinity to the artificial substrates composed of a longer moiety. The sensitivity of AP-CxTI to inhibitors was extremely reduced when compared with AP-CxTS. The insensitivity to tested organophosphates was greater than to monomethyl carbamates. AO-AChE showed similar substrate specificity and a slightly higher sensitivity to inhibitors when compared with AP-CxTS. Taking the position of Phe455Trp in the acyl pocket of the active site into account, the dimensions of the acyl pocket appear to became smaller by the substitution and insensitive to inhibitors.
ESTHER : 0h_2006_Pestic.Biochem.Physiol_85_46
PubMedSearch : 0h_2006_Pestic.Biochem.Physiol_85_46
PubMedID:

Title : Amino acid substitution in Ace paralogous acetylcholinesterase accompanied by organophosphate resistance in the spider mite Tetranychus kanzawai - Aiki_2005_Pestic.Biochem.Physiol_82_154
Author(s) : Aiki Y , Kozaki T , Mizuno H , Kono Y
Ref : Pesticide Biochemistry and Physiology , 82 :154 , 2005
Abstract : Insecticide resistant strains of the kanzawa spider mite, Tetranychus kanzawai, with insensitive AChE have spread widely throughout Japan. To clarify the molecular mechanism of this insensitivity, acetylcholinesterase (AChE) cDNA of the resistant strains of T. kanzawai was determined based on the AChE cDNA sequence of Tetranychus urticae and the sequences compared between the two spider mite species. The cDNA encoded 687 amino acids of AChE primary structure showing high homology to T. urticae. Amino acid homology indicated that the AChE is an Ace paralogous type of insect AChE. There were only three substitutions of amino acid residues between the AChEs of the two species. In the AChE of the resistant strain of T. kanzawai, one of the three amino acid substitutions was Phe439Trp, which lines the acyl pocket of the enzyme active site. Considering that the same substitution was found at the equivalent position of Ace paralogous AChE in the resistant strain of Culex tritaeniorhynchus, Phe439Trp substitution likely plays an important role in the insecticide insensitivity of the mite AChE.
ESTHER : Aiki_2005_Pestic.Biochem.Physiol_82_154
PubMedSearch : Aiki_2005_Pestic.Biochem.Physiol_82_154
PubMedID:
Gene_locus related to this paper: tetur-ACHE

Title : An amino acid substitution attributable to insecticide-insensitivity of acetylcholinesterase in a Japanese encephalitis vector mosquito, Culex tritaeniorhynchus - Nabeshima_2004_Biochem.Biophys.Res.Commun_313_794
Author(s) : Nabeshima T , Mori A , Kozaki T , Iwata Y , Hidoh O , Harada S , Kasai S , Severson DW , Kono Y , Tomita T
Ref : Biochemical & Biophysical Research Communications , 313 :794 , 2004
Abstract : A cDNA sequence encoding a Drosophila Ace-paralogous acetylcholinesterase (AChE) precursor of 701 amino acid residues was identified as the second AChE gene (Ace2) transcript from Culex tritaeniorhynchus. The Ace2 gene is tightly linked to organophosphorus insecticide (OP)-insensitivity of AChE on chromosome 2. The cDNA sequences were compared between an insecticide-susceptible strain and the resistant strain, TYM, that exhibits a 870-fold decrease in fenitroxon-sensitivity of AChE. Two amino acid substitutions were present in TYM mosquitoes. One is F455W whose homologous position in Torped AChE (Phe331) is located in the vicinity of the catalytic His in the acyl pocket of the active site gorge. The other substitution is located to a C-terminal Ile697 position that apparently seems to be excluded from the mature protein and is irrelevant to catalytic activity. The F455W replacement in the Ace2 gene is solely responsible for the insecticide-insensitivity of AChE in TYM mosquitoes.
ESTHER : Nabeshima_2004_Biochem.Biophys.Res.Commun_313_794
PubMedSearch : Nabeshima_2004_Biochem.Biophys.Res.Commun_313_794
PubMedID: 14697262
Gene_locus related to this paper: cultr-ACHE1 , cultr-ACHE2

Title : An amino acid substitution on the second acetylcholinesterase in the pirimicarb-resistant strains of the peach potato aphid, Myzus persicae - Nabeshima_2003_Biochem.Biophys.Res.Commun_307_15
Author(s) : Nabeshima T , Kozaki T , Tomita T , Kono Y
Ref : Biochemical & Biophysical Research Communications , 307 :15 , 2003
Abstract : cDNAs encoding two acetylcholinesterases (AChEs) were isolated from the peach potato aphid, Myzus persicae. MpAChE1 was orthologous and MpAChE2 was paralogous with the ace of Drosophila melanogaster. The deduced amino acid sequence of MpAChE1 cDNA was identical between the pirimicarb susceptible and resistant strains. However, a single amino acid substitution of Ser431Phe on MpAchE2 was found in the pirimicarb resistant strains. This substitution was located in the acyl pocket of the enzyme and was thought to alter the ligand specificity.
ESTHER : Nabeshima_2003_Biochem.Biophys.Res.Commun_307_15
PubMedSearch : Nabeshima_2003_Biochem.Biophys.Res.Commun_307_15
PubMedID: 12849975
Gene_locus related to this paper: myzpe-ACHE , myzpe-ACHEm

Title : Sequence of a cDNA encoding acetylcholinesterase from susceptible and resistant two-spotted spider mite, Tetranychus urticae - Anazawa_2003_Insect.Biochem.Mol.Biol_33_509
Author(s) : Anazawa Y , Tomita T , Aiki Y , Kozaki T , Kono Y
Ref : Insect Biochemistry & Molecular Biology , 33 :509 , 2003
Abstract : Acetylcholinesterase (AChE) from two-spotted spider mites, Tetranychus urticae was compared between an organophosphate susceptible (TKD) and a resistant (NCN) strain. The AChE of TKD had lower affinity to acetylthiocholine and propionylthiocholine than that of NCN, and the inhibition of AChE by DDVP, ambenonium, eserine and n-methyl-eserine showed that NCN was more insensitive than TKD. AChE cDNA sequence was determined, and the 687 amino acids of primary structure were deduced. There were six replacements of amino acid residues in TKD and two in NCN. #F331(439)C was the only substitution unique to NCN, however, this mutation existed homozygously in only two out of nine mites. This residue is one of the gorge lining components, and #F331(439)C might act an important role in the sensitivity of AChE to the inhibitors.
ESTHER : Anazawa_2003_Insect.Biochem.Mol.Biol_33_509
PubMedSearch : Anazawa_2003_Insect.Biochem.Mol.Biol_33_509
PubMedID: 12706630
Gene_locus related to this paper: tetur-ACHE

Title : Fenitroxon insensitive acetylcholinesterases of the housefly, Musca domestica associated with point mutations - Kozaki_2001_Insect.Biochem.Mol.Biol_31_991
Author(s) : Kozaki T , Shono T , Tomita T , Kono Y
Ref : Insect Biochemistry & Molecular Biology , 31 :991 , 2001
Abstract : The cDNA of AChE in the housefly, Musca domestica, was sequenced and individual flies were genotyped by this gene in an inhibition assay of AChE activity with an organophaspate, fenitroxon. Mutations at Gly(342) and Tyr(407), which are reportedly conserved in resistant strains of Drosophila, were associated with the insensitivity to fenitroxon. Two other mutations, Ile(162) and Val(260), did not have an apparent effect on insensitivity. However, the four mutations are located in the active site of the enzyme, and therefore the non-neutral mutations in this gene are considered to cause the insensitivity of AChE in the development of insecticide resistance of the housefly.
ESTHER : Kozaki_2001_Insect.Biochem.Mol.Biol_31_991
PubMedSearch : Kozaki_2001_Insect.Biochem.Mol.Biol_31_991
PubMedID: 11483435
Gene_locus related to this paper: musdo-ACHE