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).
PDF (Original Article)
- Version of Record
Restricted to System admin
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.
|Digital Object Identifier (DOI):||doi:10.1093/pcp/pcn171|
|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
|Date Deposited:||26 Oct 2011 10:40|
|Last Modified:||27 Mar 2014 19:46|
|RDF:||RDF+N-Triples, RDF+N3, RDF+XML, Browse.|
Actions (login required)