Tags

Type your tag names separated by a space and hit enter

Evolutionary diversification of aminopeptidase N in Lepidoptera by conserved clade-specific amino acid residues.
Mol Phylogenet Evol. 2014 Jul; 76:127-33.MP

Abstract

Members of the aminopepidase N (APN) gene family of the insect order Lepidoptera (moths and butterflies) bind the naturally insecticidal Cry toxins produced by the bacterium Bacillus thuringiensis. Phylogenetic analysis of amino acid sequences of seven lepidopteran APN classes provided strong support for the hypothesis that lepidopteran APN2 class arose by gene duplication prior to the most recent common ancestor of Lepidoptera and Diptera. The Cry toxin-binding region (BR) of lepidopteran and dipteran APNs was subject to stronger purifying selection within APN classes than was the remainder of the molecule, reflecting conservation of catalytic site and adjoining residues within the BR. Of lepidopteran APN classes, APN2, APN6, and APN8 showed the strongest evidence of functional specialization, both in expression patterns and in the occurrence of conserved derived amino acid residues. The latter three APN classes also shared a convergently evolved conserved residue close to the catalytic site. APN8 showed a particularly strong tendency towards class-specific conserved residues, including one of the catalytic site residues in the BR and ten others in close vicinity to the catalytic site residues. The occurrence of class-specific sequences along with the conservation of enzymatic function is consistent with the hypothesis that the presence of Cry toxins in the environment has been a factor shaping the evolution of this multi-gene family.

Authors+Show Affiliations

Department of Biological Sciences, University of South Carolina, Columbia, SC 29208, USA. Electronic address: austin@biol.sc.edu.

Pub Type(s)

Journal Article

Language

eng

PubMed ID

24675701

Citation

Hughes, Austin L.. "Evolutionary Diversification of Aminopeptidase N in Lepidoptera By Conserved Clade-specific Amino Acid Residues." Molecular Phylogenetics and Evolution, vol. 76, 2014, pp. 127-33.
Hughes AL. Evolutionary diversification of aminopeptidase N in Lepidoptera by conserved clade-specific amino acid residues. Mol Phylogenet Evol. 2014;76:127-33.
Hughes, A. L. (2014). Evolutionary diversification of aminopeptidase N in Lepidoptera by conserved clade-specific amino acid residues. Molecular Phylogenetics and Evolution, 76, 127-33. https://doi.org/10.1016/j.ympev.2014.03.014
Hughes AL. Evolutionary Diversification of Aminopeptidase N in Lepidoptera By Conserved Clade-specific Amino Acid Residues. Mol Phylogenet Evol. 2014;76:127-33. PubMed PMID: 24675701.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Evolutionary diversification of aminopeptidase N in Lepidoptera by conserved clade-specific amino acid residues. A1 - Hughes,Austin L, Y1 - 2014/03/24/ PY - 2013/10/14/received PY - 2014/03/03/revised PY - 2014/03/14/accepted PY - 2014/3/29/entrez PY - 2014/3/29/pubmed PY - 2015/1/15/medline KW - Aminopeptidase N KW - Convergent/parallel evolution KW - Diptera KW - Lepidoptera KW - Multi-gene family SP - 127 EP - 33 JF - Molecular phylogenetics and evolution JO - Mol. Phylogenet. Evol. VL - 76 N2 - Members of the aminopepidase N (APN) gene family of the insect order Lepidoptera (moths and butterflies) bind the naturally insecticidal Cry toxins produced by the bacterium Bacillus thuringiensis. Phylogenetic analysis of amino acid sequences of seven lepidopteran APN classes provided strong support for the hypothesis that lepidopteran APN2 class arose by gene duplication prior to the most recent common ancestor of Lepidoptera and Diptera. The Cry toxin-binding region (BR) of lepidopteran and dipteran APNs was subject to stronger purifying selection within APN classes than was the remainder of the molecule, reflecting conservation of catalytic site and adjoining residues within the BR. Of lepidopteran APN classes, APN2, APN6, and APN8 showed the strongest evidence of functional specialization, both in expression patterns and in the occurrence of conserved derived amino acid residues. The latter three APN classes also shared a convergently evolved conserved residue close to the catalytic site. APN8 showed a particularly strong tendency towards class-specific conserved residues, including one of the catalytic site residues in the BR and ten others in close vicinity to the catalytic site residues. The occurrence of class-specific sequences along with the conservation of enzymatic function is consistent with the hypothesis that the presence of Cry toxins in the environment has been a factor shaping the evolution of this multi-gene family. SN - 1095-9513 UR - https://www.unboundmedicine.com/medline/citation/24675701/Evolutionary_diversification_of_aminopeptidase_N_in_Lepidoptera_by_conserved_clade_specific_amino_acid_residues_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S1055-7903(14)00114-6 DB - PRIME DP - Unbound Medicine ER -