Plant Cell Advance Online Publication Published on April 29, 2005; 10.1105/tpc.105.031419
Received February 2, 2005
Returned for revision April 12, 2005
Accepted April 12, 2005
Destination-Selective Long-Distance Movement of Phloem Proteins
Koh Aoki 1*, Nobuo Suzui 2, Shu Fujimaki 2, Naoshi Dohmae 3, Keiko Yonekura-Sakakibara 1, Toru Fujiwara 2, Hiroaki Hayashi 2, Tomoyuki Yamaya 1, and Hitoshi Sakakibara 1
1 Plant Science Center, RIKEN, Institute of Physical and Chemical Research, Tsurumi, Yokohama 230-0045, Japan
2 Department of Applied Biological Chemistry, Graduate School of Agricultural and Life Sciences, University of Tokyo, Tokyo 113-8657, Japan
3 Advanced Development and Supporting Center, RIKEN, Institute of Physical and Chemical Research, Wako 351-0198, Japan
* To whom correspondence should be addressed. E-mail: kaoki{at}kazusa.or.jp.
The phloem macromolecular transport system plays a pivotal role in plant growth and development. However, little information is available regarding whether the long-distance trafficking of macromolecules is a controlled process or passive movement. Here, we demonstrate the destination-selective long-distance trafficking of phloem proteins. Direct introduction, into rice (Oryza sativa), of phloem proteins from pumpkin (Cucurbita maxima) was used to screen for the capacity of specific proteins to move long distance in rice sieve tubes. In our system, shoot-ward translocation appeared to be passively carried by bulk flow. By contrast, root-ward movement of the phloem RNA binding proteins 16-kD C. maxima phloem protein 1 (CmPP16-1) and CmPP16-2 was selectively controlled. When CmPP16 proteins were purified, the root-ward movement of CmPP16-1 became inefficient, suggesting the presence of pumpkin phloem factors that are responsible for determining protein destination. Gel-filtration chromatography and immunoprecipitation showed that CmPP16-1 formed a complex with other phloem sap proteins. These interacting proteins positively regulated the root-ward movement of CmPP16-1. The same proteins interacted with CmPP16-2 as well and did not positively regulate its root-ward movement. Our data demonstrate that, in addition to passive bulk flow transport, a destination-selective process is involved in long-distance movement control, and the selective movement is regulated by protein-protein interaction in the phloem sap.
This article has been cited by other articles:

|
 |

|
 |
 
M.-K. Lin, Y.-J. Lee, T. J. Lough, B. S. Phinney, and W. J. Lucas
Analysis of the Pumpkin Phloem Proteome Provides Insights into Angiosperm Sieve Tube Function
Mol. Cell. Proteomics,
February 1, 2009;
8(2):
343 - 356.
[Abstract]
[Full Text]
[PDF]
|
 |
|

|
 |

|
 |
 
B.-K. Ham, J. L. Brandom, B. Xoconostle-Cazares, V. Ringgold, T. J. Lough, and W. J. Lucas
A Polypyrimidine Tract Binding Protein, Pumpkin RBP50, Forms the Basis of a Phloem-Mobile Ribonucleoprotein Complex
PLANT CELL,
January 1, 2009;
21(1):
197 - 215.
[Abstract]
[Full Text]
[PDF]
|
 |
|

|
 |

|
 |
 
O. Berkowitz, R. Jost, S. Pollmann, and J. Masle
Characterization of TCTP, the Translationally Controlled Tumor Protein, from Arabidopsis thaliana
PLANT CELL,
December 1, 2008;
20(12):
3430 - 3447.
[Abstract]
[Full Text]
[PDF]
|
 |
|

|
 |

|
 |
 
C. A. Atkins and P. M. C. Smith
Translocation in Legumes: Assimilates, Nutrients, and Signaling Molecules
Plant Physiology,
June 1, 2007;
144(2):
550 - 561.
[Full Text]
[PDF]
|
 |
|

|
 |

|
 |
 
K.-i. Taoka, B.-K. Ham, B. Xoconostle-Cazares, M. R. Rojas, and W. J. Lucas
Reciprocal Phosphorylation and Glycosylation Recognition Motifs Control NCAPP1 Interaction with Pumpkin Phloem Proteins and Their Cell-to-Cell Movement
PLANT CELL,
June 1, 2007;
19(6):
1866 - 1884.
[Abstract]
[Full Text]
[PDF]
|
 |
|

|
 |

|
 |
 
A. K. Banerjee, M. Chatterjee, Y. Yu, S.-G. Suh, W. A. Miller, and D. J. Hannapel
Dynamics of a Mobile RNA of Potato Involved in a Long-Distance Signaling Pathway
PLANT CELL,
December 1, 2006;
18(12):
3443 - 3457.
[Abstract]
[Full Text]
[PDF]
|
 |
|

|
 |

|
 |
 
N. Suzui, S.-i. Nakamura, T. Fujiwara, H. Hayashi, and T. Yoneyama
A putative acyl-CoA-binding protein is a major phloem sap protein in rice (Oryza sativa L.)
J. Exp. Bot.,
August 1, 2006;
57(11):
2571 - 2576.
[Abstract]
[Full Text]
[PDF]
|
 |
|
|
|