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Published on July 11, 2008; 10.1104/pp.108.120527

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Received April 4, 2008
Accepted July 7, 2008

A Novel RNA Binding Protein Associated with Cell Plate Formation

Lian Ma , Bo Xie , Zonglie Hong *, Desh Pal S. Verma , and Zhongming Zhang *

State Key Laboratory of Agricultural Microbiology, Huazhong Agricultural University, Wuhan 430070, China; College of Life Science, Yangtze University, 88 Jingmi Road, Jingzhou 434025, China; Department of Microbiology, Molecular Biology and Biochemistry, University of Idaho, Moscow, ID 83844-3052, USA; Department of Molecular Genetics and Plant Biotechnology Center, The Ohio State University, 1060 Carmack Road, Columbus, OH 43210-1002, USA

* Corresponding author; email: zmzhang{at}mail.hzau.edu.cn.

Building a cell plate during cytokinesis in plant cells requires the participation of a number of proteins in a multistep process. We previously identified phragmoplastin as a cell plate-specific protein involved in creating a tubulo-vesicular network at the cell plate. We report here the identification and characterization of a phragmoplastin interacting protein, PHIP1, in Arabidopsis. It contains multiple functional motifs including a lysine (K)-rich domain (KRD), two RNA recognition motifs (RRMs) and three CCHC-type zinc-fingers (ZnFs). Polypeptides with similar motif structures were found only in plant protein databases, but not in the sequenced prokaryotic, fungal and animal genomes, suggesting that PHIP1 represents a plant-specific RNA-binding protein. In addition to phragmoplastin, two Arabidopsis small GTP-binding proteins, Rop1 and Ran2, are also found to interact with PHIP1. The zinc-fingers of PHIP1 were not required for its interaction with Rop1 and phragmoplastin, but may participate in its binding with the Ran2 mRNA. Immunofluorescence, in situ RNA hybridization and green fluorescence protein (GFP)-tagging experiments showed the association of PHIP1 with the forming cell plate during cytokinesis. Taken together, our data suggest that PHIP1 is a novel RNA-binding protein and may play a unique role in the polarized mRNA transport to the vicinity of the cell plate.






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