A novel RNA-binding protein associated with cell plate formation

Lian Ma; Bo Xie; Zonglie Hong; Desh Pal S Verma; Zhongming Zhang

doi:10.1104/pp.108.120527

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A novel RNA-binding protein associated with cell plate formation

Journal article

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A novel RNA-binding protein associated with cell plate formation

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

Plant physiology (Bethesda), Vol.148(1), pp.223-234

09/2008

DOI: https://doi.org/10.1104/pp.108.120527

Handle:

https://hdl.handle.net/2376/112757

PMID: 18621982

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Abstract

Protein Structure, Tertiary

Zinc Fingers

Arabidopsis - chemistry

RNA-Binding Proteins - chemistry

ras Proteins - metabolism

Guanosine Triphosphate - metabolism

Cytokinesis

Arabidopsis - metabolism

Arabidopsis Proteins - metabolism

Arabidopsis Proteins - chemistry

Membrane Proteins - metabolism

Plant Proteins - metabolism

RNA-Binding Proteins - metabolism

GTP-Binding Proteins - metabolism

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 tubulovesicular network at the cell plate. We report here the identification and characterization of a phragmoplastin-interacting protein, PHIP1, in Arabidopsis (Arabidopsis thaliana). It contains multiple functional motifs, including a lysine-rich domain, two RNA recognition motifs, and three CCHC-type zinc fingers. 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 they may participate in its binding with the Ran2 mRNA. Immunofluorescence, in situ RNA hybridization, and green fluorescent protein 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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Title: A novel RNA-binding protein associated with cell plate formation
Creators: Lian Ma - State Key Laboratory of Agricultural Microbiology, Huazhong Agricultural University, Wuhan 430070, China
Bo Xie
Zonglie Hong
Desh Pal S Verma
Zhongming Zhang
Publication Details: Plant physiology (Bethesda), Vol.148(1), pp.223-234
Academic Unit: Center for Reproductive Biology
Publisher: United States
Identifiers: 99900547467001842
Language: English
Resource Type: Journal article