کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
2015428 | 1541978 | 2007 | 11 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
A predicted N-terminal helical domain of a Group 1 LEA protein is required for protection of enzyme activity from drying
دانلود مقاله + سفارش ترجمه
دانلود مقاله ISI انگلیسی
رایگان برای ایرانیان
کلمات کلیدی
PBSGlycine-rich proteinsddH2Oisopropyl-β-d-1-thiogalactopyranosideREMIEFBCAESI-MSIPTGGSTLEABSA - BSAbovine serum albumin - آلبومین سرم گاوElectrospray Ionization Mass Spectrometry - اسپکترومتر جرم یونیزاسیون Electrospraybicinchoninic acid - بیسینکنینیک اسیدDesiccation tolerance - تحمل تخریبisoelectric focusing - تمرکز ذره ای الکتریکیtwo-dimensional - دو بعدیRelative humidity - رطوبت نسبیcircular dichroism - رنگ تابی دورانیLate embryogenesis abundant - زودرس زودرس فراوان استLate embryogenesis abundant proteins - زودرس زودرس پروتئین های فراوانMass spectroscopy - طیف سنجی جرمیPhosphate buffered saline - فسفات بافر شورlactate dehydrogenase - لاکتات دهیدروژناز LDH - لاکتات دهیدروژناز به صورت مختصر شده LDH nanometer - نانومترglutathione-S-transferase - گلوتاتیون S-ترانسفراز
موضوعات مرتبط
علوم زیستی و بیوفناوری
علوم کشاورزی و بیولوژیک
دانش گیاه شناسی
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: A predicted N-terminal helical domain of a Group 1 LEA protein is required for protection of enzyme activity from drying A predicted N-terminal helical domain of a Group 1 LEA protein is required for protection of enzyme activity from drying](/preview/png/2015428.png)
چکیده انگلیسی
Late embryogenesis abundant (LEA) proteins have been repeatedly implicated in the acquisition of desiccation tolerance in angiosperm seed embryos. However, the mechanism(s) by which protection occurs is not well understood. While the Group 1 LEA proteins are predicted to be largely unordered in solution, there is strong evidence that upon drying these proteins undergo a structural transition that leads to an increase in α-helical content. Several studies also suggest there is a direct interaction between Group 1 LEA proteins and other molecules in the cytoplasm that may be critical for the establishment of desiccation tolerance during embryo maturation. We have produced a recombinant Group 1 LEA protein and show that it is capable of protecting the enzyme lactate dehydrogenase from the deleterious effects of drying. We have also evaluated the ability of various altered recombinant Group 1 LEA proteins to protect in the same assay. Our results suggest that the highly conserved 20 amino acid Group 1 LEA signature motif is not required for protection in our in vitro assay. However, introduction of two juxtaposed proline residues into an N-terminal helical domain predicted to exist in the hydrated structure significantly compromises the ability of the recombinant protein to provide protection from drying. These results suggest that the N-terminal domain of Group 1 LEA proteins may be important for proper folding during dehydration.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Plant Physiology and Biochemistry - Volume 45, Issues 6â7, JuneâJuly 2007, Pages 389-399
Journal: Plant Physiology and Biochemistry - Volume 45, Issues 6â7, JuneâJuly 2007, Pages 389-399
نویسندگان
Gregory J. Gilles, Kelly M. Hines, Alicia J. Manfre, William R. Jr.,