AtPAP2 modulates the import of the small subunit of Rubisco into chloroplasts

Plant Signal Behav. 2016 Oct 2;11(10):e1239687. doi: 10.1080/15592324.2016.1239687.

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.

Keywords: AtPAP2; Rubisco; chloroplast; outer membrane; protein import; purple acid phosphatase; transit peptide.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Arabidopsis / enzymology*
  • Arabidopsis / genetics
  • Arabidopsis / metabolism
  • Arabidopsis Proteins / genetics
  • Arabidopsis Proteins / metabolism*
  • Biological Transport
  • Chloroplasts / genetics
  • Chloroplasts / metabolism*
  • Protein Subunits / genetics
  • Protein Subunits / metabolism*
  • Ribulose-Bisphosphate Carboxylase / genetics
  • Ribulose-Bisphosphate Carboxylase / metabolism*

Substances

  • Arabidopsis Proteins
  • Protein Subunits
  • Ribulose-Bisphosphate Carboxylase