کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
9139938 | 1163385 | 2005 | 10 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
An iron regulatory-like protein expressed in Plasmodium falciparum displays aconitase activity
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کلمات کلیدی
3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyl-2H-tetrazolium bromideIRP1ICDHIPTGDTTHsp60isopropylthiogalactosideLSCMdithiotreitolMTT - MTTIron - آهنaconitase - آکنیتازMitochondrial Deoxyribonucleic acid - اسید دهوکسی ریبونوکلئیک میتوکندریIsocitrate dehydrogenase - ایزوسیترات دهیدروژنازmtDNA - دیانای میتوکندریاییLaser scanning confocal microscopy - میکروسکوپ کانوکنال اسکن لیزرHemoglobin - هموگلوبینIron regulatory protein 1 - پروتئین تنظیم کننده آهن 1heat shock protein 60 - پروتئین شوک حرارت 60Plasmodium falciparum - پلاسمودیوم فالسیپارومTCA cycle - چرخه TCA
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شناسی مولکولی
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![عکس صفحه اول مقاله: An iron regulatory-like protein expressed in Plasmodium falciparum displays aconitase activity An iron regulatory-like protein expressed in Plasmodium falciparum displays aconitase activity](/preview/png/9139938.png)
چکیده انگلیسی
Plasmodium falciparum iron regulatory-like protein (PfIRPa) has homology to both mammalian iron regulatory proteins and aconitases and is capable of binding RNA iron response elements. We examined the subcellular localization of PfIRPa and its enzymatic properties at low oxygen tension. Differential digitonin permeabilization of isolated trophozoites with subsequent Western blot analysis suggests that the localization of PfIRPa is predominantly in the membranous compartments of the parasite, such as the mitochondrion. Immunofluorescence analysis showed that PfIRPa colocalizes with heat shock protein 60 (Hsp60), a mitochondrial marker, and is also present in the parasitic cytosol/food vacuole. Under conditions favoring the formation of an iron-sulfur cluster, recombinant PfIRPa (rPfIRPa) had aconitase activity as detected by a colorimetric NADPH-MTT (3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyl-2H-tetrazolium bromide) assay. As assessed by the hydration of cis-aconitate spectrophotometrically at 240 nm, rPfIRPa had high affinity for cis-aconitate (Km = 3.5 μM) but a low turnover number (Kcat =3.3 sâ1). The overall catalytic efficiency (Kcat/Km) of rPfIRPa was similar in magnitude to human cytosolic IRP1/aconitase and human mitochondrial aconitase. PfIRPa immunoprecipitated from parasite lysates also had aconitase activity, as assessed by an MTT-based assay. Our results provide evidence that PfIRPa localizes in the mitochondrion and in the cytosol/food vacuole and is able to demonstrate aconitase activity. Further understanding of the role of PfIRPa/aconitase in the regulation of P. falciparum homeostasis may contribute towards the development of novel antimalarial strategies against plasmodial species.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Molecular and Biochemical Parasitology - Volume 143, Issue 1, September 2005, Pages 29-38
Journal: Molecular and Biochemical Parasitology - Volume 143, Issue 1, September 2005, Pages 29-38
نویسندگان
Marcus Hodges, Emine Yikilmaz, George Patterson, Ishmael Kasvosve, Tracey A. Rouault, Victor R. Gordeuk, Mark Loyevsky,