Specific interactions between Dicer-like proteins and HYL1/DRB- family dsRNA-binding proteins in <Emphasis Type="Italic">Arabidopsis thaliana</Emphasis> |
| |
Authors: | Akihiro?Hiraguri Riku?Itoh Naoko?Kondo Yasuko?Nomura Daisuke?Aizawa Yusuke?Murai Hisashi?Koiwa Motoaki?Seki Kazuo?Shinozaki Email author" target="_blank">Toshiyuki?FukuharaEmail author |
| |
Institution: | (1) Department of Applied Biological Sciences, Tokyo University of Agriculture and Technology, Saiwaicho 3-5-8, Fuchu, Tokyo 183-8509, Japan;(2) Department of Horticultural Sciences, Texas A&M University, College Station, TX 77843-2133, USA;(3) Laboratory of Plant Molecular Biology, RIKEN Tsukuba Institute, 3-1-1 Koyadai, Tsukuba 305-0074, Japan;(4) Plant Mutation Exploration Team, Plant Functional Genomics Research Group, RIKEN Genomic Sciences Center, Yokohama 230-0045, Japan |
| |
Abstract: | Proteins that specifically bind double-stranded RNA (dsRNA) are involved in the regulation of cellular signaling events and gene expression, and are characterized by a conserved dsRNA-binding motif (dsRBM). Here we report the biochemical properties of nine such gene products, each containing one or two dsRBMs: four ArabidopsisDicer-like proteins (DCL1-4), ArabidopsisHYL1 and four of its homologs (DRB2, DRB4, DRB5 and OsDRB1). DCL1, DCL3, HYL1 and the four HYL1 homologs exhibit significant dsRNA-binding activity, indicating that these proteins are involved in RNA metabolism. The dsRBMs from dsRBM-containing proteins (dsRBPs) also function as a protein–protein interaction domain and homo- and heterodimerization are essential for biological functioning of these proteins. We show that DRB4 interacts specifically with DCL4, and HYL1 most strongly interacts with DCL1. These results indicate that each HYL1/DRB family protein interacts with one specific partner among the four Dicer-like proteins. Localization studies using GFP fusion proteins demonstrate that DCL1, DCL4, HYL1 and DRB4 localize in the nucleus, while DRB2 is present in the cytoplasm. Subcellular localizations of HYL1, DRB4, DCL1 and DCL4 further strengthen the notion that HYL1 and DCL1, and DRB4 and DCL4, exist as complexes. The presented data suggest that each member of the HYL1/DRB protein family may individually modulate Dicer function through heterodimerization with a Dicer-like protein in vivo. |
| |
Keywords: | Arabidopsis thaliana Dicer dsRNA-binding protein double-stranded RNA HYL1 protein– protein interaction |
本文献已被 PubMed SpringerLink 等数据库收录! |
|