tailieunhanh - Báo cáo khoa học: Seven-up facilitates insect counter-defense by suppressing cathepsin B expression

When challenged by the dietary soybean cysteine protease inhibitor scN, the cowpea bruchid (Callosobruchus maculatus) adapts to the inhibitory effects by readjusting the transcriptome of its digestive system, including the specific activation of a cathepsin B-like cysteine protease CmCatB. | ễFEBS Journal Seven-up facilitates insect counter-defense by suppressing cathepsin B expression Ji-Eun Ahn1 Linda A. Guarino1 2 and Keyan Zhu-Salzman1 3 1 Department of Entomology Texas A M University USA 2 Department of Biochemistry and Biophysics Texas A M University USA 3 Vegetable Fruit Improvement Center Texas A M University USA Keywords cathepsin B counter-defense COUP-TF cowpea bruchid Svp Correspondence K. Zhu-Salzman Department of Entomology Texas A M University College Station TX 77843 USA Fax 1 979 862 4790 E-mail ksalzman@ Received 24 January 2007 revised 28 March 2007 accepted 30 March 2007 doi When challenged by the dietary soybean cysteine protease inhibitor scN the cowpea bruchid Callosobruchus maculatus adapts to the inhibitory effects by readjusting the transcriptome of its digestive system including the specific activation of a cathepsin B-like cysteine protease CmCatB. To understand the transcriptional regulation of CmCatB we cloned a portion of its promoter and demonstrated its activity in Drosophila cells using a chloramphenicol acetyltransferase reporter system. EMSAs detected differential DNA-binding activity between nuclear extracts of scN-adapted and -unadapted midguts. Two tandem chicken ovalbumin upstream promoter COUP elements were identified in the CmCatB promoter that specifically interacted with a protein factor unique to nuclear extracts of unadapted insect guts where CmCatB expression was repressed. Seven-up Svp is a COUP-TF-related transcription factor that interacted with the COUP responsive element. Polyclonal anti- mosquito Svp serum abolished the specific DNA-binding activity in cowpea bruchid midgut extracts suggesting that the protein factor is an Svp homolog. Subsequent cloning of a cowpea bruchid Svp CmSvp indicated that it shares a high degree of amino acid sequence similarity with COUP-TF Svp orphan nuclear receptor family members from varied species. The protein was more abundant

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