Peroxisomal Localization of Sulfite Oxidase Separates it from Chloroplast-based Sulfur Assimilation | Zendy

Kathariowak | Zendy; Nora Luniak | Zendy; Christina Witt | Zendy; Yvonne Wüstefeld | Zendy; Andreas Wachter | Zendy; Ralf R. Mendel | Zendy; Robert Hänsch | Zendy

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Peroxisomal Localization of Sulfite Oxidase Separates it from Chloroplast-based Sulfur Assimilation

Author(s) -

Kathariowak,

Nora Luniak,

Christina Witt,

Yvonne Wüstefeld,

Andreas Wachter,

Ralf R. Mendel,

Robert Hänsch

Publication year - 2004

Publication title -

plant and cell physiology

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.975

H-Index - 152

eISSN - 1471-9053

pISSN - 0032-0781

DOI - 10.1093/pcp/pch212

Subject(s) - peroxisome , immunogold labelling , subcellular localization , peroxisomal targeting signal , biochemistry , pichia pastoris , chloroplast , microbody , protein targeting , biology , mutant , protein subcellular localization prediction , oxidase test , enzyme , microbiology and biotechnology , chemistry , gene , membrane protein , botany , recombinant dna , ultrastructure , membrane

Recently, we isolated the sulfite oxidase (SO) gene from Arabidopsis thaliana and characterized the purified SO protein. The purpose of the present study was to determine the subcellular localization of this novel plant enzyme. Immunogold electron-microscopic analysis showed the gold labels nearly exclusively in the peroxisomes. To verify this finding, green fluorescent protein was fused to full-length plant SO including the putative peroxisomal targeting signal 1 (PTS1) 'SNL' and expressed in tobacco leaves. Our results showed a punctate fluorescence pattern resembling that of peroxisomes. Co-labelling with MitoTracker-Red excluded that the observed fluorescence was due to mitochondrial sorting. By investigation of deleted or mutated PTS1, no functional peroxisomal targeting signal 2 (PTS2) could be detected in plant SO. This conclusion is supported by expression studies in Pichia pastoris mutants with defined defects either in PTS1- or PTS2-mediated peroxisomal import.

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