TAILIEUCHUNG - Báo cáo khoa học: Enzymatic control of anhydrobiosis-related accumulation of trehalose in the sleeping chironomid, Polypedilum vanderplanki

Larvae of an anhydrobiotic insect,Polypedilum vanderplanki, accumulate very large amounts of trehalose as a compatible solute on desiccation, but the molecular mechanisms underlying this accumulation are unclear. We therefore isolated the genes coding for trehalose metabolism enzymes, . | ỊFEBS Journal Enzymatic control of anhydrobiosis-related accumulation of trehalose in the sleeping chironomid Polypedilum vanderplanki IX I It D 1 X z I IX 1 It It I . lix . 1 l-x I 1 I 1 Kanako Mitsumasu Yasushi Kanamori Mika Fujita Ken-ichi Iwata Daisuke Tanaka Shingo Kikuta2 Masahiko Watanabe1 Richard Cornette1 Takashi Okuda1 and Takahiro Kikawada1 1 Anhydrobiosis Research Unit National institute of AgrobiologicalSciences Tsukuba Ibaraki Japan 2 Department of Integrated Biosciences Graduate Schoolof Frontier Sciences The University of Tokyo Japan Keywords anhydrobiosis trehalase trehalose trehalose-6-phosphate phosphatase trehalose-6-phosphate synthase Correspondence T. Kikawada and T. Okuda National institute of AgrobiologicalSciences NIAS Ohwashi 1-2 Tsukuba Ibaraki 305-8634 Japan Fax 81 29 838 6157 Tel 81 29 838 6170 E-mail kikawada@ oku@ Database Nucleotide sequence data for PvTps PvTpsa PvTpsb PvTpp PvTreh and PvGp are available in the EMBL GenBank DDBJ databases under the accession numbers AB490331 AB490332 AB490333 AB490334 AB490335 and AB490336 respectively Re-use of this article is permitted in accordance with the Terms and Conditions set out at http onlineopen OnlineOpen_Terms Received 25 May 2010 revised 6 August 2010 accepted 9 August 2010 doi Larvae of an anhydrobiotic insect Polypedilum vanderplanki accumulate very large amounts of trehalose as a compatible solute on desiccation but the molecular mechanisms underlying this accumulation are unclear. We therefore isolated the genes coding for trehalose metabolism enzymes . trehalose-6-phosphate synthase TPS and trehalose-6-phosphate phosphatase TPP for the synthesis step and trehalase TREH for the degradation step. Although computational prediction indicated that the alternative splicing variants PvTpsa b obtained encoded probable functional motifs consisting of a typical consensus domain of TPS and a conserved sequence

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