Perinuclear and nuclear envelope localizations of <Emphasis Type="Italic">Arabidopsis</Emphasis> Ran proteins |
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Authors: | Lian Ma Zonglie Hong Zhongming Zhang |
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Institution: | (1) State Key Laboratory of Agricultural Microbiology, Huazhong Agricultural University, Wuhan, 430070, China;(2) College of Life Science, Yangtze University, Jingzhou, 434025, China;(3) Department of Microbiology, Molecular Biology and Biochemistry, University of Idaho, Moscow, ID 83844, USA |
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Abstract: | Using phragmoplastin-interacting protein 1 (PhrIP1) as bait, we isolated an Arabidopsis cDNA encoding Ran2, a small Ras-like GTP-binding protein. The interaction between PhrIP1 and Ran2 was confirmed by an in
vitro protein–protein interaction assay with purified Ran2 and PhrIP1. The plant Ran2 shares high sequence homology, 78 and
86% at the amino acid level, with human Ran/TC4 and C.
elegans Ran, respectively. Our results obtained from enzyme assays and Western blot analysis show that Ran2 has intrinsic GTPase
activity and is present in the soluble fraction of Arabidopsis seedling extract. Fluorescent microscopy using anti-Ran2 antibody revealed that the Ran protein is localized in the perinuclear
region with the highest concentration at the nuclear envelope. In contrast to its animal counterparts that are present in
the nucleoplasm, the Ran protein is absent inside the nucleus. These results suggest that plant Ran proteins may be involved
in mediation of nucleocytoplasmic transport and assembly of the nuclear envelope after karyokinesis in plant cells. |
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Keywords: | Arabidopsis thaliana GTPase Phragmoplastin Nuclear envelope Cell division Cytokinesis |
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