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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), pp. 1917-1921. (doi:10.1093/pcp/pcn171). (PMID:19001421).

Record type: Article


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.

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e-pub ahead of print date: 10 November 2008
Published date: December 2008
Keywords: arabidopsis thaliana and Pisum sativum, imerization, gtpase, ph sensitivity, protein translocation, toc
Organisations: Centre for Biological Sciences


Local EPrints ID: 200515
ISSN: 0032-0781
PURE UUID: 96726927-32fb-47f8-99f2-10678197b6ce
ORCID for Ivo Tews: ORCID iD

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Date deposited: 26 Oct 2011 10:40
Last modified: 18 Jul 2017 11:14

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Author: Tihana Bionda
Author: Patrick Koenig
Author: Mislav Oreb
Author: Ivo Tews ORCID iD
Author: Enrico Schleiff

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