Peroxisomal plant nitric oxide synthase (NOS) protein is imported by peroxisomal targeting signal type 2 (PTS2) in a process that depends on the cytosolic receptor PEX7 and calmodulin.

Francisco J Corpas, Juan B Barroso

Journal: FEBS letters 2014;588(12):2049-54

PMID: 24801177

Abstract

Nitric oxide (NO) production in plant peroxisomes by l-arginine-dependent NO synthase activity has been proven. The PEX5 and PEX7 PTS receptors, which recognize PTS1- and PTS2-containing proteins, are localized in the cytosol. Using AtPex5p and AtPex7p knockdown in Arabidopsis by RNA interference (RNAi) designated as pex5i and pex7i, we found that the l-arginine-dependent protein responsible for NO generation in peroxisomes appears to be imported through an N-terminal PTS2. Pharmacological analyzes using a calcium channel blocker and calmodulin (CaM) antagonist show that the import of the peroxisomal NOS protein also depends on calcium and calmodulin.

Address: Group of Antioxidants, Free Radicals and Nitric Oxide in Biotechnology, Food and Agriculture, Department of Biochemistry, Cell and Molecular Biology of Plants, Estación Experimental del Zaidín, CSIC, Apartado 419, E-18080 Granada, Spain. Electronic address: [email protected].; Group of Biochemistry and Cell Signaling in Nitric Oxide, Department of Biochemistry and Molecular Biology, University of Jaén, Campus "Las Lagunillas", E-23071 Jaén, Spain.

DOI: 10.1016/j.febslet.2014.04.034

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MeSH Terms: Arabidopsis, Arabidopsis Proteins, Calcium, Calmodulin, Cytosol, Mutation, Nitric Oxide, Nitric Oxide Synthase, Peroxisomal Targeting Signal 2 Receptor, Peroxisomes, Protein Transport, RNA Interference, Receptors, Cytoplasmic and Nuclear