Structural considerations of folded protein import through the chloroplast TOC/TIC translocons

FEBS Letters

article

Iniyan Ganesan¹  Steven M. Theg¹ 

[1] Department of Plant Biology, University of California Davis

关键词: BamA;    chloroplast protein import;    Sam50;    TIC;    TOC;   

DOI  :  10.1002/1873-3468.13342

来源: John Wiley & Sons Ltd.

【 摘 要 】

Protein import into chloroplasts is carried out by the protein translocons at the outer and inner envelope membranes (TOC and TIC). Detailed structures for these translocons are lacking, with only a low-resolution TOC complex structure available. Recently, we showed that the TOC/TIC translocons can import folded proteins, a rather unique feat for a coupled double membrane system. We also determined the maximum functional TOC/TIC pore size to be 30–35 A. Here, we discuss how such large pores could form and compare the structural dynamics of the pore-forming Toc75 subunit to its bacterial/mitochondrial Omp85 family homologs. We put forward structural models that can be empirically tested and also briefly review the pore dynamics of other protein translocons with known structures.

【 授权许可】

Unknown