Please use this identifier to cite or link to this item:
|Title:||Molecular insights into miRNA processing by Arabidopsis thaliana SERRATE|
Adam Yuan, Y.
|Citation:||MacHida, S., Chen, H.-Y., Adam Yuan, Y. (2011-09). Molecular insights into miRNA processing by Arabidopsis thaliana SERRATE. Nucleic Acids Research 39 (17) : 7828-7836. ScholarBank@NUS Repository. https://doi.org/10.1093/nar/gkr428|
|Abstract:||In plant, primary transcripts (pri-miRNAs) transcribed from miRNA genes by RNA polymerase II are first processed into stem-loop pre-miRNAs and further chopped into ∼21nt long miRNAs by RNase III-like enzyme DCL1. SERRATE (SE) protein is an essential component for miRNA processing by assisting DCL1 for accurate cleavage. Here we report the crystal structure of Arabidopsis SE core (residues 194-543) at 2.7 Å. SE core adopts the 'walking man-like' topology with N-terminal α helices, C-terminal non-canonical zinc-finger domain and novel Middle domain resembling the leading leg, the lagging leg and the body, respectively. Pull-down assay shows that SE core provides the platform for HYL1 and DCL1 binding, whereas in vitro RNA binding and in vivo mutant rescue experiments suggest that the non-canonical zinc-finger domain coupled with C-terminal tail binds miRNA precursors. SE presumably works as a scaffold-like protein capable of binding both protein and RNA to guide the positioning of miRNA precursor toward DCL1 catalytic site within miRNA processing machinery in plant. © 2011 The Author(s).|
|Source Title:||Nucleic Acids Research|
|Appears in Collections:||Staff Publications|
Show full item record
Files in This Item:
There are no files associated with this item.
checked on Nov 14, 2018
WEB OF SCIENCETM
checked on Nov 7, 2018
checked on Oct 12, 2018
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.