AtPAP2 modulates the import of the small subunit of Rubisco into chloroplasts. (2nd October 2016)

• Record Type: Journal Article
• Authors: Zhang, Renshan; Guan, Xiaoqian; Law, Yee-Song; Sun, Feng; Chen, Shuai; Wong, Kam Bo; Lim, Boon Leong
• Is Part Of: Plant signaling & behavior. Volume 11:Number 10(2016)
• Publication Date: 2016-10-02
• Subjects: AtPAP2 -- chloroplast -- outer membrane -- protein import -- purple acid phosphatase -- Rubisco -- transit peptide; Plant ecophysiology -- Periodicals; Plant cellular signal transduction -- Periodicals; Plant cellular signal transduction; Plant ecophysiology; Periodicals; Electronic journals; 581
• DOI: 10.1080/15592324.2016.1239687
• Languages: English
• ISSNs: 1559-2316

Abstract

ABSTRACT: Arabidopsis thaliana purple acid phosphatase 2 (AtPAP2) is the only phosphatase that is dual-targeted to both chloroplasts and mitochondria. Like Toc33/34 of the TOC and Tom 20 of the TOM, AtPAP2 is anchored to the outer membranes of chloroplasts and mitochondria via a hydrophobic C-terminal motif. AtPAP2 on the mitochondria was previously shown to recognize the presequences of several nuclear-encoded mitochondrial proteins and modulate the import of pMORF3 into the mitochondria. Here we show that AtPAP2 binds to the small subunit of Rubisco (pSSU) and that chloroplast import experiments demonstrated that pSSU was imported less efficiently into pap2 chloroplasts than into wild-type chloroplasts. We propose that AtPAP2 is an outer membrane-bound phosphatase receptor that facilitates the import of selected proteins into chloroplasts.