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Molecular characterisation of a candidate gut sucrase in the pea aphid, Acyrthosiphon pisum

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JournalInsect Biochemistry and Molecular Biology
DatePublished - Apr 2007
Issue number4
Volume37
Number of pages11
Pages (from-to)307-317
Original languageEnglish

Abstract

The hydrolysis of sucrose, the principal dietary source of carbon for aphids, is catalysed by a gut alpha-glucosidase/transglucosidase activity. An alpha-glucosidase, referred to as APS1, was identified in both a gut-specific cDNA library and a sucrase-enriched membrane preparation from guts of the pea aphid Acyrthosiphon pisum by a combination of genomic and proteomic techniques. APS1 contains a predicted signal peptide, and has a predicted molecular mass of 68 kDa (unprocessed) or 66.4 kDa (mature protein). It has amino acid sequence similarity to alpha-glucosidases (EC 3.2.1.20) of glycoside hydrolase family 13 in other insects. The predicted APS1 protein contains two domains: an N-terminal catalytic domain, and a C-terminal hydrophobic domain. In situ localisation and RT-PCR studies revealed that APS1 mRNA was expressed in the gut distal to the stomach, the same localisation as sucrase activity. When expressed heterologously in Xenopus embryos, APS1 was membrane-bound and had sucrase activity. It is concluded that APS1 is a dominant, and possibly sole, protein mediating sucrase activity in the aphid gut. (c) 2007 Published by Elsevier Ltd.

    Research areas

  • Acyrthosiphon pisum, aphid, alpha-glucosidase, digestive enzyme, phloem-feeding insect, sucrase, PHLOEM-FEEDING INSECT, PERIMICROVILLAR MEMBRANES, NEISSERIA-POLYSACCHAREA, HONEYDEW, OSMOREGULATION, MIDGUT, SUCROSE, OLIGOSACCHARIDES, AMYLOSUCRASE, PROTEINS

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