期刊
JOURNAL OF CELL SCIENCE
卷 125, 期 21, 页码 5196-5207出版社
COMPANY OF BIOLOGISTS LTD
DOI: 10.1242/jcs.111054
关键词
Endoplasmic reticulum; HSP90; Post-translational import; Arabidopsis thaliana
类别
资金
- Deutsche Forschungsgemeinschaft [SFB 1035, A04, GRK 845]
- Fonds der chemischen Industrie [Do 187/22]
Chaperone-assisted sorting of post-translationally imported proteins is a general mechanism among all eukaryotic organisms. Interaction of some preproteins with the organellar membranes is mediated by chaperones, which are recognised by membrane-bound tetratricopeptide repeat (TPR) domain containing proteins. We have characterised AtTPR7 as an endoplasmic reticulum protein in plants and propose a potential function for AtTPR7 in post-translational protein import. Our data demonstrate that AtTPR7 interacts with the heat shock proteins HSP90 and HSP70 via a cytosol-exposed TPR domain. We further show by in vitro and in vivo experiments that AtTPR7 is associated with the Arabidopsis Sec63 homologue, AtERdj2. Interestingly, AtTPR7 can functionally complement a Delta sec71 yeast mutant that is impaired in post-translational protein transport. These data strongly suggest that AtTPR7 not only has a role in chaperone binding but also in post-translational protein import into the endoplasmic reticulum, pointing to a general mechanism of chaperone-mediated post-translational sorting between the endoplasmic reticulum, mitochondria and chloroplasts in plant cells.
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