pH sensitivity of the GTPase Toc33 as a regulatory circuit for protein translocation into chloroplasts


Bionda, Tihana, Koenig, Patrick, Oreb, Mislav, Tews, Ivo and Schleiff, Enrico (2008) pH sensitivity of the GTPase Toc33 as a regulatory circuit for protein translocation into chloroplasts. Plant and Cell Physiology, 49, (12), 1917-1921. (doi:10.1093/pcp/pcn171). (PMID:19001421).

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Description/Abstract

The properties of membrane-embedded GTPases are investigated to understand translocation of preprotein across the outer envelope of chloroplasts. The homo- and heterodimerization events of the GTPases had been established previously. 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 between homo- and heterodimeric conformations.

Item Type: Article
ISSNs: 0032-0781 (print)
1471-9053 (electronic)
Keywords: arabidopsis thaliana and Pisum sativum, imerization, gtpase, ph sensitivity, protein translocation, toc
Subjects: Q Science > QP Physiology
Divisions: Faculty of Natural and Environmental Sciences > Biological Sciences
ePrint ID: 200515
Date Deposited: 26 Oct 2011 10:40
Last Modified: 27 Mar 2014 19:46
URI: http://eprints.soton.ac.uk/id/eprint/200515

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