کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
4570463 1332038 2013 11 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Crystal Structure of Arabidopsis thaliana Dawdle Forkhead-Associated Domain Reveals a Conserved Phospho-Threonine Recognition Cleft for Dicer-Like 1 Binding
موضوعات مرتبط
علوم زیستی و بیوفناوری علوم کشاورزی و بیولوژیک دانش گیاه شناسی
پیش نمایش صفحه اول مقاله
Crystal Structure of Arabidopsis thaliana Dawdle Forkhead-Associated Domain Reveals a Conserved Phospho-Threonine Recognition Cleft for Dicer-Like 1 Binding
چکیده انگلیسی

ABSTRACTDawdle (DDL) is a microRNA processing protein essential for the development of Arabidopsis. DDL contains a putative nuclear localization signal at its amino-terminus and forkhead-associated (FHA) domain at the carboxyl-terminus. Here, we report the crystal structure of the FHA domain of Arabidopsis Dawdle, determined by multiple-wavelength anomalous dispersion method at 1.7-Å resolution. DDL FHA structure displays a seven-stranded β-sandwich architecture that contains a unique structural motif comprising two long anti-parallel strands. Strikingly, crystal packing of the DDL FHA domain reveals that a glutamate residue from the symmetry-related DDL FHA domain, a structural mimic of the phospho-threonine, is specifically recognized by the structurally conserved phospho-threonine binding cleft. Consistently with the structural observations, co-immuno-precipitation experiments performed in Nicotiana benthamiana show that the DDL FHA domain co-immuno-precipitates with DCL1 fragments containing the predicted pThr+3(Ile/Val/Leu/Asp) motif. Taken together, we count the recognition of the target residue by the canonical binding cleft of the DDL FHA domain as the key molecular event to instate FHA domain-mediated protein–protein interaction in plant miRNA processing.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: - Volume 6, Issue 4, July 2013, Pages 1290–1300
نویسندگان
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