Structure of arabidopsis Hyponastic Leaves1 and its molecular implications for miRNA Processing

Seong Wook Yang, Hong Ying Chen, Jing Yang, Satoru Machida, Nam Hai Chua, Y. Adam Yuan

Research output: Contribution to journalArticle

89 Citations (Scopus)

Abstract

The Arabidopsis HYPONASTIC LEAVES1 (HYL1) is a double-stranded RNA-binding protein that forms a complex with DICER-LIKE1 (DCL1) and SERRATE to facilitate processing of primary miRNAs into microRNAs (miRNAs). However, the structural mechanisms of miRNA maturation by this complex are poorly understood. Here, we present the crystal structures of double-stranded RNA binding domains (dsRBD1 and dsRBD2) of HYL1 and HYL1 dsRBD1 (HR1)/dsRNA complex as well as human TRBP2 dsRBD2 (TR2)/dsRNA complex for comparison analysis. Structural and functional study demonstrates that both HR1 and TR2 are canonical dsRBDs for dsRNA binding, whereas HR2 of HYL1 is a non-canonical dsRBD harboring a putative dimerization interface. Domain swapping within the context of HYL1 demonstrates that TR2 can supplant the function of HR1 in vitro and in vivo. Further biochemical analyses suggest that HYL1 probably binds to the miRNA/miRNA* region of precursors as a dimer mediated by HR2.

Original languageEnglish
Pages (from-to)594-605
Number of pages12
JournalStructure
Volume18
Issue number5
DOIs
Publication statusPublished - 2010 May 1

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MicroRNAs
Arabidopsis
RNA-Binding Proteins
Dimerization
Double-Stranded RNA Binding Motif

All Science Journal Classification (ASJC) codes

  • Structural Biology
  • Molecular Biology

Cite this

Yang, Seong Wook ; Chen, Hong Ying ; Yang, Jing ; Machida, Satoru ; Chua, Nam Hai ; Yuan, Y. Adam. / Structure of arabidopsis Hyponastic Leaves1 and its molecular implications for miRNA Processing. In: Structure. 2010 ; Vol. 18, No. 5. pp. 594-605.
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Structure of arabidopsis Hyponastic Leaves1 and its molecular implications for miRNA Processing. / Yang, Seong Wook; Chen, Hong Ying; Yang, Jing; Machida, Satoru; Chua, Nam Hai; Yuan, Y. Adam.

In: Structure, Vol. 18, No. 5, 01.05.2010, p. 594-605.

Research output: Contribution to journalArticle

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