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|Title:||Crystal structure of arabidopsis thaliana dawdle forkhead-associated domain reveals a conserved phospho-threonine recognition cleft for dicer-like 1 binding||Authors:||Machida, S.
|Issue Date:||Jul-2013||Citation:||Machida, S., Yuan, Y.A. (2013-07). Crystal structure of arabidopsis thaliana dawdle forkhead-associated domain reveals a conserved phospho-threonine recognition cleft for dicer-like 1 binding. Molecular Plant 6 (4) : 1290-1300. ScholarBank@NUS Repository. https://doi.org/10.1093/mp/sst007||Abstract:||Dawdle (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. © 2013 The Author.||Source Title:||Molecular Plant||URI:||http://scholarbank.nus.edu.sg/handle/10635/100360||ISSN:||16742052||DOI:||10.1093/mp/sst007|
|Appears in Collections:||Staff Publications|
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