Plant and Cell Physiology Advance Access published online on November 10, 2008
Plant and Cell Physiology, doi:10.1093/pcp/pcn171
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pH sensitivity of the GTPase Toc33 as a regulatory circuit for protein translocation into chloroplasts
1 JWGU Frankfurt am Main, Cluster of Excellence Macromolecular Complexes, Center of Membrane Proteomics, Department of Biosciences, Molecular Cell Biology, Max-von-Laue Str. 9, 60439 Frankfurt, Germany; 2 Heidelberg University Biochemistry Centre, Im Neuenheimer Feld 328, 69120 Heidelberg, Germany;
Corresponding author: Prof. Enrico Schleiff, Molecular Cell Biology of Plants, Biocenter, N 200, 3. OG, Max-von-Laue-Str. 9, D-60438 Frankfurt/Main, Germany, Tel. 0049-69 798-29284, Fax 0049-69 798-29286, e-mail: schleiff{at}bio.uni-frankfurt.de
| Abstract |
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Properties of membrane embedded GTPases are investigated to understand translocation of preproteins across the outer envelope of chloroplasts. The homo- and hetero-dimerization events of the GTPases were previously established. We show that the hydrolytic activity of the GTPase Toc33 is pH insensitive in the homodimeric conformation but has a bell shaped pH optimum in the monomeric conformation. Further, Toc33 GTPase homodimerization and protein translocation into chloroplasts are pH sensitive as well. pH sensitivity might serve to regulate translocation; alternatively, the documented pH-sensitivity might reflect a mechanistic requirement for GTPase silencing during translocation as the GTPase switches homo- to hetrodimeric conformations.
Keywords: Arabidopsis thaliana and Pisum sativum - dimerization - GTPase - pH sensitivity - protein translocation - TOC
* Both authors contributed to the same extent
(Received October 20, 2008; Accepted October 31, 2008)
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