pH sensitivity of the GTPase Toc33 as a regulatory circuit for protein translocation into chloroplasts
pH sensitivity of the GTPase Toc33 as a regulatory circuit for protein translocation into chloroplasts
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.
arabidopsis thaliana and Pisum sativum, imerization, gtpase, ph sensitivity, protein translocation, toc
1917-1921
Bionda, Tihana
d3a07ba5-d51b-4eb9-8e04-88cfc52ac3f6
Koenig, Patrick
e03428c5-67ef-4df4-9310-77190d216517
Oreb, Mislav
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Tews, Ivo
9117fc5e-d01c-4f8d-a734-5b14d3eee8dd
Schleiff, Enrico
119114bb-9cbb-45e9-a161-db45b1e9f4ba
December 2008
Bionda, Tihana
d3a07ba5-d51b-4eb9-8e04-88cfc52ac3f6
Koenig, Patrick
e03428c5-67ef-4df4-9310-77190d216517
Oreb, Mislav
85bcf606-2b7c-4362-a88f-b99bf6cbe748
Tews, Ivo
9117fc5e-d01c-4f8d-a734-5b14d3eee8dd
Schleiff, Enrico
119114bb-9cbb-45e9-a161-db45b1e9f4ba
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), .
(doi:10.1093/pcp/pcn171).
(PMID:19001421)
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.
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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
Identifiers
Local EPrints ID: 200515
URI: http://eprints.soton.ac.uk/id/eprint/200515
ISSN: 0032-0781
PURE UUID: 96726927-32fb-47f8-99f2-10678197b6ce
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Date deposited: 26 Oct 2011 10:40
Last modified: 15 Mar 2024 03:36
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Author:
Tihana Bionda
Author:
Patrick Koenig
Author:
Mislav Oreb
Author:
Enrico Schleiff
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