کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10753237 | 1050337 | 2014 | 6 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Biochemical and structural characterization of an endoplasmic reticulum-localized late embryogenesis abundant (LEA) protein from the liverwort Marchantia polymorpha
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کلمات کلیدی
IPTGLEAER localizationMarchantia polymorphaisopropyl β-D-1-thiogalactopyranoside - ایزوپروپیل β-D-1-thiogalactopyranosideCho - برایDesiccation tolerance - تحمل تخریبChinese Hamster Ovary - تخمدان هامستر چینیcircular dichroism - رنگ تابی دورانیLate embryogenesis abundant - زودرس زودرس فراوان استendoplasmic reticulum - شبکه آندوپلاسمی FT-IR - طیف سنجی مادون قرمز تبدیل فوریهfourier transform-infrared - فوریه تبدیل مادون قرمزLEA proteins - پروتئین LEAIntrinsically disordered protein - پروتئین ناسازگار ذاتی
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
Late embryogenesis abundant (LEA) proteins, which accumulate to high levels in seeds during late maturation, are associated with desiccation tolerance. A member of the LEA protein family was found in cultured cells of the liverwort Marchantia polymorpha; preculture treatment of these cells with 0.5 M sucrose medium led to their acquisition of desiccation tolerance. We characterized this preculture-induced LEA protein, designated as MpLEA1. MpLEA1 is predominantly hydrophilic with a few hydrophobic residues that may represent its putative signal peptide. The protein also contains a putative endoplasmic reticulum (ER) retention sequence, HEEL, at the C-terminus. Microscopic observations indicated that GFP-fused MpLEA1 was mainly localized in the ER. The recombinant protein MpLEA1 is intrinsically disordered in solution. On drying, MpLEA1 shifted predominantly toward α-helices from random coils. Such changes in conformation are a typical feature of the group 3 LEA proteins. Recombinant MpLEA1 prevented the aggregation of α-casein during desiccation-rehydration events, suggesting that MpLEA1 exerts anti-aggregation activity against desiccation-sensitive proteins by functioning as a “molecular shield”. Moreover, the anti-aggregation activity of MpLEA1 was ten times greater than that of BSA or insect LEA proteins, which are known to prevent aggregation on drying. Here, we show that an ER-localized LEA protein, MpLEA1, possesses biochemical and structural features specific to group 3 LEA proteins.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochemical and Biophysical Research Communications - Volume 454, Issue 4, 28 November 2014, Pages 588-593
Journal: Biochemical and Biophysical Research Communications - Volume 454, Issue 4, 28 November 2014, Pages 588-593
نویسندگان
Rie Hatanaka, Takao Furuki, Tempei Shimizu, Daisuke Takezawa, Takahiro Kikawada, Minoru Sakurai, Yasutake Sugawara,