Arabidopsis Profilin Isoforms, PRF1 and PRF2 Show Distinctive Binding Activities and Subcellular Distributions

  1. Feng Wang1,†,
  2. Yanping Jing2,3,†,
  3. Zhen Wang2,
  4. Tonglin Mao1,
  5. Jozef Šamaj4,5,
  6. Ming Yuan1,*,
  7. Haiyun Ren2,*

Article first published online: 20 JAN 2009

DOI: 10.1111/j.1744-7909.2008.00781.x

Issue

Journal of Integrative Plant Biology

Journal of Integrative Plant Biology

Volume 51, Issue 2, pages 113–121, February 2009

Additional Information

How to Cite

Wang, F., Jing, Y., Wang, Z., Mao, T., Šamaj, J., Yuan, M. and Ren, H. (2009), Arabidopsis Profilin Isoforms, PRF1 and PRF2 Show Distinctive Binding Activities and Subcellular Distributions. Journal of Integrative Plant Biology, 51: 113–121. doi: 10.1111/j.1744-7909.2008.00781.x

Author Information

  1. 1

    State Key Laboratory of Plant Physiology and Biochemistry, China Agricultural University, Beijing 100094, China

  2. 2

    College of Life Sciences, Beijing Normal University, Beijing 100875, China

  3. 3

    College of Biological Sciences and Biotechnology, Beijing Forestry University, Beijing 100083, China

  4. 4

    Institute of Cellular and Molecular Botany, Rheinische Friedrich-Wilhelms- University Bonn, Department of Plant Cell Biology, Kirschallee 1, D-53115 Bonn, Germany

  5. 5

    Institute of Plant Genetics and Biotechnology, Slovak Academy of Sciences, Akademicka 2, SK-95007, Nitra, Slovak Republic)

  1. †

    These authors share first authorship.

* *Authors for correspondence. Tel: +86 10 5880 6090; E-mail: <hren@bnu.edu.cn>. Tel: +86 10 6273 3436; E-mail: <mingyuan@cau.edu.cn>.

Publication History

  1. Issue published online: 20 JAN 2009
  2. Article first published online: 20 JAN 2009
  3. Received 18 Mar. 2008  Accepted 19 Jun. 2008

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Keywords:

  • actin filaments;
  • Arabidopsis;
  • endoplasmic reticulum;
  • profilin isoforms;
  • PRF1;
  • PRF2

Abstract

Profilin is an actin-binding protein that shows complex effects on the dynamics of the actin cytoskeleton. There are five profilin isoforms in Arabidopsis thaliana L. However, it is still an open question whether these isoforms are functionally different. In the present study, two profilin isoforms from Arabidopsis, PRF1 and PRF2 were fused with green fluorescent protein (GFP) tag and expressed in Escherichia coli and A. thaliana in order to compare their biochemical properties in vitro and their cellular distributions in vivo. Biochemical analysis revealed that fusion proteins of GFP-PRF1 and GFP-PRF2 can bind to poly-L-proline and G-actin showing remarkable differences. GFP-PRF1 has much higher affinities for both poly-L-proline and G-actin compared with GFP-PRF2. Observations of living cells in stable transgenic A. thaliana lines revealed that 35S::GFP-PRF1 formed a filamentous network, while 35S::GFP-PRF2 formed polygonal meshes. Results from the treatment with latrunculin A and a subsequent recovery experiment indicated that filamentous alignment of GFP-PRF1 was likely associated with actin filaments. However, GFP-PRF2 localized to polygonal meshes resembling the endoplasmic reticulum. Our results provide evidence that Arabidopsis profilin isoforms PRF1 and PRF2 have different biochemical affinities for poly-L-proline and G-actin, and show distinctive localizations in living cells. These data suggest that PRF1 and PRF2 are functionally different isoforms.

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