Structure of Arabidopsis HYPONASTIC LEAVES1 and Its Molecular Implications for miRNA Processing

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...

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Published inStructure (London) Vol. 18; no. 5; pp. 594 - 605
Main Authors Yang, Seong Wook, Chen, Hong-Ying, Yang, Jing, Machida, Satoru, Chua, Nam-Hai, Yuan, Y. Adam
Format Journal Article
LanguageEnglish
Published United States Elsevier Inc 12.05.2010
Subjects
ARABIDOPSIS
Arabidopsis - genetics
Arabidopsis - metabolism
BASIC BIOLOGICAL SCIENCES
Binding
Biochemistry
Biomedical materials
CRYSTAL STRUCTURE
DEAD-box RNA Helicases - genetics
DEAD-box RNA Helicases - metabolism
DIMERIZATION
DIMERS
FUNCTIONALS
GENERAL AND MISCELLANEOUS//MATHEMATICS, COMPUTING, AND INFORMATION SCIENCE
Humans
IN VITRO
IN VIVO
In vivo testing
In vivo tests
MicroRNAs - genetics
MicroRNAs - metabolism
Molecular structure
national synchrotron light source
Precursors
PROCESSING
PROTEINS
Ribonuclease III - genetics
Ribonuclease III - metabolism
RNA
RNA Interference
RNA, Double-Stranded - genetics
RNA, Double-Stranded - metabolism
RNA-Binding Proteins - chemistry
RNA-Binding Proteins - genetics
RNA-Binding Proteins - metabolism
RNA
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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. ► Crystal structures of dsRBD1 and dsRBD2 of HYL1 (HR1 and HR2) and dsRBD2 of TRBP2 (TR2) ► Crystal structures of HR1/dsRNA and TR2/dsRNA complexes ► Chimerical TR2-HR2 protein rescues HYL1 function in vitro and in vivo ► HYL1 probably binds to miRNA/miRNA ∗ region of precursors as a dimer mediated by HR2
AbstractList 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.
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 micro-RNAs (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.
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 super(*) region of precursors as a dimer mediated by HR2.
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. ► Crystal structures of dsRBD1 and dsRBD2 of HYL1 (HR1 and HR2) and dsRBD2 of TRBP2 (TR2) ► Crystal structures of HR1/dsRNA and TR2/dsRNA complexes ► Chimerical TR2-HR2 protein rescues HYL1 function in vitro and in vivo ► HYL1 probably binds to miRNA/miRNA ∗ region of precursors as a dimer mediated by HR2
Author Yang, Seong Wook
Machida, Satoru
Chua, Nam-Hai
Yang, Jing
Chen, Hong-Ying
Yuan, Y. Adam
AuthorAffiliation 3 Department of Biological Sciences, National University of Singapore, 14 Science Drive 4, Singapore 117543, Singapore
1 Host-Pathogen Interaction Group, Temasek Life Sciences Laboratory, National University of Singapore, 1 Research Link, Singapore 117604, Singapore
2 Laboratory of Plant Molecular Biology, The Rockefeller University, New York, NY 10065, USA
4 Structural Biology Group, Temasek Life Sciences Laboratory, National University of Singapore, 1 Research Link, Singapore 117604, Singapore
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BackLink https://www.ncbi.nlm.nih.gov/pubmed/20462493$$D View this record in MEDLINE/PubMed
https://www.osti.gov/biblio/1019858$$D View this record in Osti.gov
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Snippet The Arabidopsis HYPONASTIC LEAVES1 (HYL1) is a double-stranded RNA-binding protein that forms a complex with DICER-LIKE1 (DCL1) and SERRATE to facilitate...
The Arabidopsis HYPONASTIC LEAVES1 (HYL1) is a double-stranded RNA-binding protein that forms a complex with DICER-LIKE1 (DCL1) and SERRATE to facilitate...
The Arabidopsis HYPONASTIC LEAVES1 (HYL1) is a double-stranded RNA-binding protein that forms a complex with DICER-LIKE1 (DCL1) and SERRATE to facilitate...
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SubjectTerms ARABIDOPSIS
Arabidopsis - genetics
Arabidopsis - metabolism
BASIC BIOLOGICAL SCIENCES
Binding
Biochemistry
Biomedical materials
CRYSTAL STRUCTURE
DEAD-box RNA Helicases - genetics
DEAD-box RNA Helicases - metabolism
DIMERIZATION
DIMERS
FUNCTIONALS
GENERAL AND MISCELLANEOUS//MATHEMATICS, COMPUTING, AND INFORMATION SCIENCE
Humans
IN VITRO
IN VIVO
In vivo testing
In vivo tests
MicroRNAs - genetics
MicroRNAs - metabolism
Molecular structure
national synchrotron light source
Precursors
PROCESSING
PROTEINS
Ribonuclease III - genetics
Ribonuclease III - metabolism
RNA
RNA Interference
RNA, Double-Stranded - genetics
RNA, Double-Stranded - metabolism
RNA-Binding Proteins - chemistry
RNA-Binding Proteins - genetics
RNA-Binding Proteins - metabolism
Title Structure of Arabidopsis HYPONASTIC LEAVES1 and Its Molecular Implications for miRNA Processing
URI https://dx.doi.org/10.1016/j.str.2010.02.006
https://www.ncbi.nlm.nih.gov/pubmed/20462493
https://search.proquest.com/docview/1671296019
https://search.proquest.com/docview/733516191
https://search.proquest.com/docview/745932704
https://www.osti.gov/biblio/1019858
https://pubmed.ncbi.nlm.nih.gov/PMC3119452
Volume 18
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