Cytosolic targeting factor AKR2A captures chloroplast outer membrane-localized client proteins at the ribosome during translation

Dae Heon Kim, Jae-Eun Lee, Zheng-Yi Xu, Kyoung Rok Geem, Yun Kwon, Joon Won Park () and Inhwan Hwang ()
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Dae Heon Kim: Pohang University of Science and Technology
Jae-Eun Lee: Pohang University of Science and Technology
Zheng-Yi Xu: Pohang University of Science and Technology
Kyoung Rok Geem: Pohang University of Science and Technology
Yun Kwon: Pohang University of Science and Technology
Joon Won Park: Pohang University of Science and Technology
Inhwan Hwang: Pohang University of Science and Technology

Nature Communications, 2015, vol. 6, issue 1, 1-13

Abstract: Abstract In eukaryotic cells, organellar proteome biogenesis is pivotal for cellular function. Chloroplasts contain a complex proteome, the biogenesis of which includes post-translational import of nuclear-encoded proteins. However, the mechanisms determining when and how nascent chloroplast-targeted proteins are sorted in the cytosol are unknown. Here, we establish the timing and mode of interaction between ankyrin repeat-containing protein 2 (AKR2A), the cytosolic targeting factor of chloroplast outer membrane (COM) proteins, and its interacting partners during translation at the single-molecule level. The targeting signal of a nascent AKR2A client protein residing in the ribosomal exit tunnel induces AKR2A binding to ribosomal RPL23A. Subsequently, RPL23A-bound AKR2A binds to the targeting signal when it becomes exposed from ribosomes. Failure of AKR2A binding to RPL23A in planta severely disrupts protein targeting to the COM; thus, AKR2A-mediated targeting of COM proteins is coupled to their translation, which in turn is crucial for biogenesis of the entire chloroplast proteome.

Date: 2015
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DOI: 10.1038/ncomms7843

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