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J Biol Chem. 2009 Jul 10;284(28):19132-41. doi: 10.1074/jbc.M109.012831. Epub 2009 May 12.

Interaction of actin and the chloroplast protein import apparatus.

Author information

1
Department of Plant Sciences, University of Cambridge, Downing Street, Cambridge CB2 3EA, United Kingdom.

Abstract

Actin filaments are major components of the cytoskeleton and play numerous essential roles, including chloroplast positioning and plastid stromule movement, in plant cells. Actin is present in pea chloroplast envelope membrane preparations and is localized at the surface of the chloroplasts, as shown by agglutination of intact isolated chloroplasts by antibodies to actin. To identify chloroplast envelope proteins involved in actin binding, we have carried out actin co-immunoprecipitation and co-sedimentation experiments on detergent-solubilized pea chloroplast envelope membranes. Proteins co-immunoprecipitated with actin were identified by mass spectrometry and by Western blotting and included the Toc159, Toc75, Toc34, and Tic110 components of the TOC-TIC protein import apparatus. A direct interaction of actin with Escherichia coli-expressed Toc159, but not Toc33, was shown by co-sedimentation experiments, suggesting that Toc159 is the component of the TOC complex that interacts with actin on the cytosolic side of the outer envelope membrane. The physiological significance of this interaction is unknown, but it may play a role in the import of nuclear-encoded photosynthesis proteins.

PMID:
19435889
PMCID:
PMC2707226
DOI:
10.1074/jbc.M109.012831
[Indexed for MEDLINE]
Free PMC Article

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