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

Price, D.R.G., Karley, A.J., Ashford, D.A., Isaacs, H.V., Pownall, M.E., Wilkinson, H.S., Gatehouse, J.A. and Douglas, A.E. (2007) Molecular characterisation of a candidate gut sucrase in the pea aphid, Acyrthosiphon pisum. Insect Biochemistry and Molecular Biology, 37 (4). pp. 307-317. ISSN 0965-1748

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The hydrolysis of sucrose, the principal dietary source of carbon for aphids, is catalysed by a gut α-glucosidase/transglucosidase activity. An α-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 α-glucosidases (EC 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.

Item Type: Article
Institution: The University of York
Academic Units: The University of York > Biology (York)
Depositing User: York RAE Import
Date Deposited: 24 Jul 2009 14:26
Last Modified: 24 Jul 2009 14:26
Published Version: http://dx.doi.org/10.1016/j.ibmb.2006.12.005
Status: Published
Publisher: Elsevier
Identification Number: 10.1016/j.ibmb.2006.12.005
URI: http://eprints.whiterose.ac.uk/id/eprint/6354

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