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Open Access Research article

Fusion to GFP blocks intercellular trafficking of the sucrose transporter SUT1 leading to accumulation in companion cells

Sylvie Lalonde1*, Andreas Weise14, Rama Panford Walsh1, John M Ward12 and Wolf B Frommer13

Author Affiliations

1 ZMBP Tübingen, Plant Physiology, Auf der Morgenstelle 1, D-72076 Tübingen, Germany

2 Current address: Plant Biology Dept., University of Minnesota, 1445 Gortner Ave., St. Paul, MN 55108-1095, USA

3 Current address: Carnegie Institution, 260 Panama Street, Stanford, California 94305, USA

4 Current address: Greenovation Biotech GmbH, Boetzinger Str. 29 b, D-79111 Freiburg, Germany

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BMC Plant Biology 2003, 3:8  doi:10.1186/1471-2229-3-8

Published: 11 December 2003

Abstract

Background

Plant phloem consists of an interdependent cell pair, the sieve element / companion cell complex. Sucrose transporters are localized to enucleate sieve elements (SE), despite being transcribed in companion cells (CC). Due to the high turnover of SUT1, sucrose transporter mRNA or protein must traffic from CC to SE via the plasmodesmata. Localization of SUT mRNA at plasmodesmatal orifices connecting CC and SE suggests RNA transport, potentially mediated by RNA binding proteins. In many organisms, polar RNA transport is mediated through RNA binding proteins interacting with the 3'-UTR and controlling localized protein synthesis. To study mechanisms for trafficking of SUT1, GFP-fusions with and without 3'-UTR were expressed in transgenic plants.

Results

In contrast to plants expressing GFP from the strong SUC2 promoter, in RolC-controlled expression GFP is retained in companion cells. The 3'-UTR of SUT1 affected intracellular distribution of GFP but was insufficient for trafficking of SUT1, GFP or their fusions to SEs. Fusion of GFP to SUT1 did however lead to accumulation of SUT1-GFP in the CC, indicating that trafficking was blocked while translational inhibition of SUT1 mRNA was released in CCs.

Conclusion

A fusion with GFP prevents targeting of the sucrose transporter SUT1 to the SE while leading to accumulation in the CC. The 3'-UTR of SUT1 is insufficient for mobilization of either the fusion or GFP alone. It is conceivable that SUT1-GFP protein transport through PD to SE was blocked due to the presence of GFP, resulting in retention in CC particles. Alternatively, SUT1 mRNA transport through the PD could have been blocked due to insertion of GFP between the SUT1 coding sequence and 3'-UTR.