کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10840278 | 1067621 | 2005 | 5 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
DNA mismatch binding activities in Chlorella pyrenoidosa extracts and affinity isolation of G-T mismatch binding proteins
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کلمات کلیدی
2-DEMSADNA mismatchPMSFPMFDTTMALDI-TOFMS/MS - MS / MSElectrophoretic mobility shift assay - آزمون تحرک تحرک الکتروفورزPeptide mass fingerprinting - اثر انگشت پپتیدهSDS-PAGE - الکتروفورز ژل پلی آکریل آمیدSodium dodecyl sulfate polyacrylamide gel electrophoresis - الکتروفورز ژل پلی اتیل آمید سدیم دودسیل سولفاتAffinity adsorption - جذب وابستگیtwo-dimensional - دو بعدیdithiothreitol - دیتیوتریتولmatrix-assisted laser desorption ionization-time of flight - زمان یونیزاسیون لیزر جذب لیزر ماتریس-زمان پروازphenylmethylsulfonyl fluoride - فنیل متیل سولفونیل فلورایدIsoelectric point - نقطه ایزوالکتریکBinding proteins - پروتئین های اتصالCHAPS - چاپسChlorella pyrenoidosa - کلرلا پیرنوییدا
موضوعات مرتبط
علوم زیستی و بیوفناوری
علوم کشاورزی و بیولوژیک
دانش گیاه شناسی
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
DNA mismatch recognition proteins contained in the extracts of unicellular alga Chlorella pyrenoidosa were isolated by affinity adsorption and 2-D gel electrophoresis. Incubation of the algal extracts with a 38-mer duplex oligonucleotide carrying a single DNA simple mispair generated a few gel retardation complexes. G-T mispair was recognized significantly better than C-T, G-G, G-A, and C-C mispairs by the algal extracts and these extracts bound very weakly to G-A and C-C mispairs, displaying a universal trend of mismatch binding efficiency. The levels of mismatch recognition complexes were slightly increased in the presence of 1Â mM ATP. Two 13-kDa G-T binding polypeptides possessing pIs of 5.3 and 5.5 were isolated after resolving affinity-captured proteins by 2-D gel electrophoresis and the two factors were found to bind 5.5- and 2.8-fold stronger to heteroduplex than to homoduplex DNA, respectively. No proteins significantly homologous to the two algal G-T binding proteins were found by peptide mass fingerprinting (PMF). The sequence of a peptide generated from trypsin-cleavage of one G-T binding factor (pI 5.5) could be aligned with the amino acid sequences that form the C-terminal active sites of human and mouse mismatch-specific uracil/thymine-DNA glycosylases, suggesting the possibility of this factor as an algae- or a Chlorella-specific DNA mismatch glycosylase.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Plant Physiology and Biochemistry - Volume 43, Issue 4, April 2005, Pages 309-313
Journal: Plant Physiology and Biochemistry - Volume 43, Issue 4, April 2005, Pages 309-313
نویسندگان
Todd Hsu, Kai-Ning Chang, Yi-Show Lai, Ting-Yi Jung, Gen-I Lee,