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atToc33 is a transit peptide receptor of the chloroplast outer envelope membrane, and possesses GTPase activity. In vitro, its transit peptide- and GTP-binding properties are abrogated by its phosphorylation at serine 181, which was proposed to represent an important regulatory mechanism. We mutated S181 to alanine (to prevent phosphorylation), and to aspartate and glutamate (to mimic the effects of phosphoserine), and expressed all three proteins in ppi1 (atToc33 knockout) plants using the native promoter. The mutants complemented ppi1 with equal efficiency in respect of all criteria tested, including protein import efficiency and light stress tolerance. The data suggest that atToc33 phosphorylation may not play an important role in vivo.

Original publication

DOI

10.1016/j.febslet.2005.12.055

Type

Journal article

Journal

FEBS Lett

Publication Date

23/01/2006

Volume

580

Pages

649 - 655

Keywords

Arabidopsis, Arabidopsis Proteins, Chloroplasts, Genotype, Light, Membrane Proteins, Mutation, Phenotype, Phosphorylation, Plants, Genetically Modified, Promoter Regions, Genetic