Non-native, N-terminal Hsp70 molecular motor recognition elements in transit peptides support plastid protein translocation.

ABSTRACT: Previously, we identified the N-terminal domain of transit peptides (TPs) as a major determinant for the translocation step in plastid protein import. Analysis of Arabidopsis TP dataset revealed that this domain has two overlapping characteristics, highly uncharged and Hsp70-interacting. To investigate these two properties, we replaced the N-terminal domains of the TP of the small subunit of ribulose-1,5-bisphosphate carboxylase/oxygenase and its reverse peptide with a series of unrelated peptides whose affinities to the chloroplast stromal Hsp70 have been determined. Bioinformatic analysis indicated that eight out of nine peptides in this series are not similar to the TP N terminus. Using in vivo and in vitro protein import assays, the majority of the precursors containing Hsp70-binding e

SUBMITTER: Chotewutmontri P 

PROVIDER: S-EPMC4367265 | biostudies-literature | 2015 Mar

REPOSITORIES: biostudies-literature