Please use this identifier to cite or link to this item:
https://doi.org/10.1093/mp/sst007
DC Field | Value | |
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dc.title | Crystal structure of arabidopsis thaliana dawdle forkhead-associated domain reveals a conserved phospho-threonine recognition cleft for dicer-like 1 binding | |
dc.contributor.author | Machida, S. | |
dc.contributor.author | Yuan, Y.A. | |
dc.date.accessioned | 2014-10-27T08:24:57Z | |
dc.date.available | 2014-10-27T08:24:57Z | |
dc.date.issued | 2013-07 | |
dc.identifier.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 | |
dc.identifier.issn | 16742052 | |
dc.identifier.uri | http://scholarbank.nus.edu.sg/handle/10635/100360 | |
dc.description.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. | |
dc.source | Scopus | |
dc.subject | Arabidopsis DCL1 | |
dc.subject | Arabidopsis DDL | |
dc.subject | forkhead-associated domain | |
dc.subject | microRNA processing. | |
dc.subject | phospho-threonine | |
dc.type | Article | |
dc.contributor.department | BIOLOGICAL SCIENCES | |
dc.description.doi | 10.1093/mp/sst007 | |
dc.description.sourcetitle | Molecular Plant | |
dc.description.volume | 6 | |
dc.description.issue | 4 | |
dc.description.page | 1290-1300 | |
dc.identifier.isiut | 000322410700021 | |
Appears in Collections: | Staff Publications |
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