کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10748650 | 1050276 | 2016 | 26 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Characterization of the binding between a 70-kDa heat shock protein, HspA1A, and phosphoinositides
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کلمات کلیدی
PI(3,5)P2NBDLVSSGChsp70PI(3,4)P2SBDPhosphatidylinositol 4-phosphate - Phosphatidylinositol 4-فسفاتPI(3)P - PI (3) PPI(3,4,5)P3 - PI (3،4،5) P3PI(4)P - PI (4) PPI(4,5)P2 - PI (4،5) P2Stress - استرس یا فشار روانیSDS-PAGE - الکتروفورز ژل پلی آکریل آمیدSodium dodecyl sulfate polyacrylamide gel electrophoresis - الکتروفورز ژل پلی اتیل آمید سدیم دودسیل سولفاتsubstrate-binding domain - دامنه اتصال به بسترnucleotide-binding domain - دامنه اتصال دهنده نوکلئوتیدیSulfatide - سولفاتیمMembranes - غشاءphosphatidylinositol - فسفاتیدیل اینوزیتولphosphatidylcholine - فسفاتیدیل کولینPhosphatidylserine - فسفاتیدیلسرینphosphatidylinositol (3,4,5)-triphosphate - فسفاتیدیلینواستول (3،4،5) تری فسفاتphosphatidylinositol 3,4-bisphosphate - فسفاتیدیلینواستیل 3،4-بیسفسفاتphosphatidylinositol 3-phosphate - فسفاتیدیلینوزیتول 3-فسفاتPhosphatidylinositol 3,5-bisphosphate - فسفاتیدیلینوزیتول 3،5-بیسفسفاتphosphatidylinositol 4,5-bisphosphate - فسفاتیدیلینوزیتول 4،5-بیسفسفاتPhosphatidylinositol 5-phosphate - فسفاتیدیلینوزیتول 5-فسفاتLiposomes - لیپوزومBMP - مدیریت فرایند کسب و کارHeat-shock proteins - پروتئین های شوک حرارتLipid-binding - چسبندگی لیپیدیCardiolipin - کاردیولیپین
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
HspA1A, a seventy-kilodalton heat shock protein, binds to specific anionic lipids and this interaction regulates important physiological phenomena like apoptosis, tumor growth, and lysosomal rescue. However, whether HspA1A binds to phosphoinositides has yet to be established and quantified. Therefore, in this study, we determined the binding affinity of HspA1A to several phosphoinositides and characterized five aspects of their molecular interaction. First, we established that HspA1A binds phosphatidylinositol monophosphates with higher affinity than di- and triphosphorylated inositides. Second, using high concentrations of potassium we found that HSPA1A embeds within the lipid bilayer of all phosphoinositides tested. However, the effects of the high salt concentrations were significantly different between the different phosphoinositides. Third, using calcium and reaction buffers equilibrated at different pH values we found that these differentially affected HspA1A-phosphoinositide binding, revealing a lipid-specific pattern of binding. Fourth, by assessing the binding properties of the two HspA1A domains, the nucleotide-binding domain and the substrate-binding domain, we determined that in most cases the full-length protein is necessary for binding to phosphoinositides. Fifth, by including in the reactions nucleotides and protein substrates we determined that they minimally and differentially affected phosphoinositide-binding. Collectively, these findings strongly suggest that the HspA1A-phosphoinositide binding is complex yet specific, is mediated by both electrostatic and hydrophobic interactions, is not related to the lipid-head charge, and depends on the physicochemical properties of the lipid.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochemical and Biophysical Research Communications - Volume 472, Issue 1, 25 March 2016, Pages 270-275
Journal: Biochemical and Biophysical Research Communications - Volume 472, Issue 1, 25 March 2016, Pages 270-275
نویسندگان
Chelsea McCallister, Brianna Kdeiss, Ryan Oliverio, Nikolas Nikolaidis,