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JXB Advance Access originally published online on January 30, 2004
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Journal of Experimental Botany, Vol. 55, No. 397, pp. 595-604, March 1, 2004
© 2004 Oxford University Press

Cell and Molecular Biology, Biochemistry and Molecular Physiology

GFP-labelled Rubisco and aspartate aminotransferase are present in plastid stromules and traffic between plastids

Received 4 September 2003; Accepted 10 November 2003

Ernest Y. Kwok and Maureen R. Hanson*

Department of Molecular Biology and Genetics, 321 Biotechnology Building, Cornell University, Ithaca, NY 14853, USA

* To whom correspondence should be addressed. Fax: +1 607 255 6249. E-mail: mrh5{at}cornell.edu
Abbreviations: AAT, aspartate aminotransferase; AAT3, plastid aspartate aminotransferase; CFP, cyan fluorescent protein; FRAP, fluorescence recovery after photobleaching; GFP, green fluorescent protein; LS, large subunit of Rubisco; L8S8, Rubisco holoenzyme; NPC, nuclear pore complex; Rubisco, ribulose-1,5-bisphosphate carboxylase/oxygenase; SDS-PAGE, denaturing polyacrylamide gel electrophoresis; SS, small subunit of Rubisco.

Plastid stromules are membrane-bound protrusions of the plastid envelope that contain soluble stroma. Stromules are often found connecting plastids within a cell and fluorescence recovery after photobleaching (FRAP) experiments have demonstrated that green fluorescent protein (GFP) can move between plastids via these connections. In this report, the ability of endogenous plastid proteins to travel through stromules was investigated. The motility of GFP-labelled plastid aspartate aminotransferase and the Rubisco small subunit was studied in stromules by FRAP. Both fusion proteins assemble into protein complexes that appear to behave similarly to their endogenous counterparts. In addition, both enzymes are capable of trafficking between plastids via stromules.

Key words: Aspartate aminotransferase, chloroplast, FRAP, photobleaching, plastid, protein trafficking, Rubisco, stromule.


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