کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
5506238 | 1400289 | 2017 | 6 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Expression and characterization of the Plasmodium translocon of the exported proteins component EXP2
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کلمات کلیدی
1,2-dioleoyl-sn-glycero-3-phospho-l-serineDOPSBLMDOPCRBCppmGSTIPTGTransloconHlyEDDMPEXELβ-d-1-thiogalactopyranosidePBS1,2-dioleoyl-sn-glycero-3-phosphocholine - 1،2-dioleoyl-sn-glycero-3-phosphocholine1,2-dioleoyl-sn-glycero-3-phosphoethanolamine - 1،2-dioleoyl-sn-glycero-3-phosphoethanolamineHRV - ENGn-dodecyl-β-d-maltopyranoside - n-dodecyl-β-D-maltopyranosideBlue native PAGE - PAGE آبی بومیsphingomyelin - اسفنگومیلینblue native polyacrylamide gel electrophoresis - الکتروفورز ژل پلی آکریل آمید آبی بومیTem - این استPVM - تاریخHuman rhinovirus - رینوویروس انسانیparasite plasma membrane - غشای پلاسمای انگلیbilayer lipid membrane - غشای چربی دو طرفهMalaria - مالاریاPhosphate-buffered saline - محلول نمک فسفات با خاصیت بافریTransmission electron microscopy - میکروسکوپ الکترونی عبوریparasitophorous vacuole - واکسن پارازیتوفورPore-forming protein - پروتئین تشکیل دهنده پوستهPlasmodium - پلاسمودیم، انگل مالاریاDOPE - پیش بینی کردنChannel - کانالred blood cell - گلبول قرمز، اریتروسیتglutathione S-transferase - گلوتاتیون S-ترانسفراز
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
The malaria parasite Plasmodium falciparum requires the Plasmodium translocon of exported proteins (PTEX) to proliferate in human red blood cells. During the blood stages of malaria, several hundred parasite-encoded proteins are exported from the parasite into the cytosol of red blood cells. PTEX is the translocon for protein export and comprises 5 proteins: EXP2, PTEX150, PTEX88, Hsp101 and TRX2. Among them, EXP2 is thought to constitute the transmembrane pore, whereas the other components seem to play a role in unfolding the luggage proteins or providing a driving force. However, detailed functional and structural characterizations of PTEX proteins have not been performed. In this study, we expressed and characterized the membrane-associated component EXP2. Because expression of EXP2 is lethal to E. coli, EXP2 was expressed as a fusion protein with GST, and the recombinant EXP2 was obtained by protease digestion. The recombinant EXP2 formed pores in bilayer lipid membranes. The inner diameter of the pore was estimated to be approximately 3.5 nm based on electron microscopy images and channel currents. From this size and the molecular mass as determined by size exclusion chromatography and blue native polyacrylamide gel electrophoresis, we determined that the pore comprises approximately 10-12 EXP2 subunits. However, there is a possibility that the pore structure is different in the PTEX complex. These results provide important insights in the protein transport mechanism of PTEX, which will aid in developing new drugs targeting PTEX.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochemical and Biophysical Research Communications - Volume 482, Issue 4, 22 January 2017, Pages 700-705
Journal: Biochemical and Biophysical Research Communications - Volume 482, Issue 4, 22 January 2017, Pages 700-705
نویسندگان
Kazuaki Hakamada, Hirokazu Watanabe, Ryuji Kawano, Keiichi Noguchi, Masafumi Yohda,