کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10752643 | 1050329 | 2015 | 6 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Heat shock transcription factor δ32 is targeted for degradation via an ubiquitin-like protein ThiS in Escherichia coli
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کلمات کلیدی
IPTGHSRCBBisopropyl-β-d-thiogalactosideCoomassie Brilliant Blue - Coomassie درخشان آبیEscherichia coli - اشریشیا کُلیUbiquitin-proteasome system - سیستم Ubiquitin-proteasomeCo-IP - شرکت-IPHeat shock response - پاسخ شوک گرماUbiquitin-like proteins - پروبیوتیک های مشابه ابیکتینUbiquitin-like protein - پروتئین مانند پروتئین UbiquitinUPS - یو پی اس
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
The posttranslational modification of proteins with ubiquitin and ubiquitin-like proteins (UBLs) plays an important role in eukaryote biology, through which substrate proteins are targeted for degradation by the proteasome. Prokaryotes have been thought to degrade proteins by an ubiquitin independent pathway. Here, we show that ThiS, an ubiquitin-like protein, is covalently attached to δ32 and at least 27 other proteins, leading to their subsequent degradation by proteases, in a similar manner to the ubiquitin-proteasome system (UPS) in eukaryotes. Molecular biology and biochemical studies confirm that specific lysine sites in δ32 can be modified by ThiS. The results presented here establish a new model for δ32 degradation and show that Escherichia coli uses a small-protein modifier to control protein stability.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochemical and Biophysical Research Communications - Volume 459, Issue 2, 3 April 2015, Pages 240-245
Journal: Biochemical and Biophysical Research Communications - Volume 459, Issue 2, 3 April 2015, Pages 240-245
نویسندگان
Xibing Xu, Yulong Niu, Ke Liang, Jianmei Wang, Xufeng Li, Yi Yang,