کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10537077 | 962666 | 2009 | 7 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Effects of recombinant protein misfolding and aggregation on bacterial membranes
دانلود مقاله + سفارش ترجمه
دانلود مقاله ISI انگلیسی
رایگان برای ایرانیان
کلمات کلیدی
IPTGGSTTLCNPNPFLDPH1,6-diphenyl-1,3,5-hexatriene - 1،6-دیفنیل-1،3،5-هگزیدریلFT–IR - FT-IRisopropyl β-D-1-thiogalactopyranoside - ایزوپروپیل β-D-1-thiogalactopyranosideinclusion body - بدن درگیرprotein aggregation - تجمع پروتئینSOD - سدSuperoxide dismutase - سوکسوکس دیسموتازFourier transform infrared spectroscopy - طیف سنجی مادون قرمز تبدیل فوریه یا طیف سنجی FTIRMembrane lipid - غشای چربیStress metabolism - متابولیسم استرسElectron microscopy - میکروسکوپ الکترونیRecombinant protein - پروتئین های نوترکیبthin-layer chromatography - کروماتوگرافی نازک لایهglutathione-S-transferase - گلوتاتیون S-ترانسفراز
موضوعات مرتبط
مهندسی و علوم پایه
شیمی
شیمی آنالیزی یا شیمی تجزیه
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
The expression of recombinant proteins is known to induce a metabolic rearrangement in the host cell. We used aggregation-sensitive model systems to study the effects elicited in Escherichia coli cells by the aggregation of recombinant glutathione-S-transferase and its fusion with the green fluorescent protein that, according to the expression conditions, accumulate intracellularly as soluble protein, or soluble and insoluble aggregates. We show that the folding state of the recombinant protein and the complexity of the intracellular aggregates critically affect the cell response. Specifically, protein misfolding and aggregation induce changes in specific host proteins involved in lipid metabolism and oxidative stress, a reduction in the membrane permeability, as well as a rearrangement of its lipid composition. The temporal evolution of the host cell response and that of the aggregation process pointed out that the misfolded protein and soluble aggregates are responsible for the membrane modifications and the changes in the host protein levels. Interestingly, native recombinant protein and large insoluble aggregates do not seem to activate stress markers and membrane rearrangements.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics - Volume 1794, Issue 2, February 2009, Pages 263-269
Journal: Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics - Volume 1794, Issue 2, February 2009, Pages 263-269
نویسندگان
D. Ami, A. Natalello, T. Schultz, P. Gatti-Lafranconi, M. Lotti, S.M. Doglia, A. de Marco,