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Molecular identification and characterization of rhodaneses from the insect herbivore Pieris rapae.
Steiner, Anna-Maria; Busching, Christine; Vogel, Heiko; Wittstock, Ute.
Affiliation
  • Steiner AM; Institute of Pharmaceutical Biology, Technische Universität Braunschweig, Mendelssohnstr. 1, 38106, Braunschweig, Germany.
  • Busching C; Institute of Pharmaceutical Biology, Technische Universität Braunschweig, Mendelssohnstr. 1, 38106, Braunschweig, Germany.
  • Vogel H; Department of Entomology, Max Planck Institute for Chemical Ecology, Hans-Knöll-Str. 8, 07745, Jena, Germany.
  • Wittstock U; Institute of Pharmaceutical Biology, Technische Universität Braunschweig, Mendelssohnstr. 1, 38106, Braunschweig, Germany. u.wittstock@tu-bs.de.
Sci Rep ; 8(1): 10819, 2018 Jul 17.
Article in En | MEDLINE | ID: mdl-30018390
ABSTRACT
The association of cabbage white butterflies (Pieris spec., Lepidoptera Pieridae) with their glucosinolate-containing host plants represents a well-investigated example of the sequential evolution of plant defenses and insect herbivore counteradaptations. The defensive potential of glucosinolates, a group of amino acid-derived thioglucosides present in plants of the Brassicales order, arises mainly from their rapid breakdown upon tissue disruption resulting in formation of toxic isothiocyanates. Larvae of P. rapae are able to feed exclusively on glucosinolate-containing plants due to expression of a nitrile-specifier protein in their gut which redirects glucosinolate breakdown to the formation of nitriles. The release of equimolar amounts of cyanide upon further metabolism of the benzylglucosinolate-derived nitrile suggests that the larvae are also equipped with efficient means of cyanide detoxification such as ß-cyanoalanine synthases or rhodaneses. While insect ß-cyanoalanine synthases have recently been identified at the molecular level, no sequence information was available of characterized insect rhodaneses. Here, we identify and characterize two single-domain rhodaneses from P. rapae, PrTST1 and PrTST2. The enzymes differ in their kinetic properties, predicted subcellular localization and expression in P. rapae indicating different physiological roles. Phylogenetic analysis together with putative lepidopteran rhodanese sequences indicates an expansion of the rhodanese family in Pieridae.
Subject(s)

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Thiosulfate Sulfurtransferase / Butterflies / Insect Proteins Type of study: Diagnostic_studies Limits: Animals Language: En Journal: Sci Rep Year: 2018 Document type: Article Affiliation country: Alemania

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Thiosulfate Sulfurtransferase / Butterflies / Insect Proteins Type of study: Diagnostic_studies Limits: Animals Language: En Journal: Sci Rep Year: 2018 Document type: Article Affiliation country: Alemania