Chloroplast Outer Membrane ß-Barrel Proteins Use Components of the General Import Apparatus.
Plant Cell
; 31(8): 1845-1855, 2019 08.
Article
em En
| MEDLINE
| ID: mdl-31217220
ABSTRACT
Chloroplasts evolved from a cyanobacterial endosymbiont that resided within a eukaryotic cell. Due to their prokaryotic heritage, chloroplast outer membranes contain transmembrane ß-barrel proteins. While most chloroplast proteins use N-terminal transit peptides to enter the chloroplasts through the translocons at the outer and inner chloroplast envelope membranes (TOC/TIC), only one ß-barrel protein, Toc75, has been shown to use this pathway. The route other ß-barrel proteins use has remained unresolved. Here we use in vitro pea (Pisum sativum) chloroplast import assays and transient expression in Nicotiana benthamiana to address this. We show that a paralog of Toc75, outer envelope protein 80 kD (OEP80), also uses a transit peptide but has a distinct envelope sorting signal. Our results additionally indicate that ß-barrels that do not use transit peptides also enter the chloroplast using components of the general import pathway.
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Cloroplastos
/
Arabidopsis
/
Proteínas de Arabidopsis
/
Proteínas de Cloroplastos
Idioma:
En
Revista:
Plant Cell
Assunto da revista:
BOTANICA
Ano de publicação:
2019
Tipo de documento:
Article