NDLI: A toc159 import receptor mutant, defective in hydrolysis of GTP, supports preprotein import into chloroplasts.

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A toc159 import receptor mutant, defective in hydrolysis of GTP, supports preprotein import into chloroplasts.

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A toc159 import receptor mutant, defective in hydrolysis of GTP, supports preprotein import into chloroplasts.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Wang, Fei Kessler, Felix Hwang, Inhwan Hofstetter, Valère Lee, Dong Wook Martin, Meryll Agne, Birgit Schnell, Danny Infanger, Sibylle Rahim, Gwendoline
Description	Author Affiliation: Agne B ( Laboratoire de Physiologie Végétale, Université de Neuchâtel, Rue Emile-Argand 11, 2007 Neuchâtel, Switzerland.)
Abstract	The heterotrimeric Toc core complex of the chloroplast protein import apparatus contains two GTPases, Toc159 and Toc34, together with the protein-conducting channel Toc75. Toc159 and Toc34 are exposed at the chloroplast surface and function in preprotein recognition. Together, they have been shown to facilitate the import of photosynthetic proteins into chloroplasts in Arabidopsis. Consequently, the ppi2 mutant lacking atToc159 has a non-photosynthetic albino phenotype. Previous mutations in the conserved G1 and G3 GTPase motifs abolished the function of Toc159 in vivo by disrupting targeting of the receptor to chloroplasts. Here, we demonstrate that a mutant in a conserved G1 lysine (atToc159 K868R) defective in GTP binding and hydrolysis can target and assemble into Toc complexes. We show that atToc159 K868R can support protein import into isolated chloroplasts, albeit at lower preprotein binding and import efficiencies compared with the wild-type receptor. Considering the absence of measurable GTPase activity in the K868R mutant, we conclude that GTP hydrolysis at atToc159 is not strictly required for preprotein translocation. The data also indicate that preprotein import requires at least one additional GTPase other than Toc159.
ISSN	00219258
e-ISSN	1083351X
Journal	Journal of Biological Chemistry
Issue Number	13
Volume Number	284
Language	English
Publisher	American Society for Biochemistry and Molecular Biology (United States)
Publisher Date	2009-03-27
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Arabidopsis Proteins Metabolism Arabidopsis Enzymology Chloroplasts GTP Phosphohydrolases Guanosine Triphosphate Membrane Proteins Mutation Amino Acid Motifs Physiology Genetics Hydrolysis Protein Precursors Protein Transport Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Biochemistry Molecular Biology
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

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