Sorting pathway and molecular targeting signals for the Arabidopsis peroxin 3
Autor: | Richard N. Trelease, Joanne E Hunt |
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Rok vydání: | 2004 |
Předmět: |
Saccharomyces cerevisiae Proteins
Time Factors Recombinant Fusion Proteins Molecular Sequence Data Arabidopsis Biophysics Peroxin Biology Biochemistry Peroxins Chloramphenicol acetyltransferase Epitopes Cytosol Tobacco Peroxisomes Amino Acid Sequence Molecular Biology Peroxisomal targeting signal Peptide sequence Expressed Sequence Tags Sequence Homology Amino Acid Arabidopsis Proteins Peroxisomal matrix Cell Membrane fungi Membrane Proteins Cell Biology Peroxisome biology.organism_classification Protein Structure Tertiary Cell biology Transmembrane domain Phenotype ATP-Binding Cassette Transporters Protein Processing Post-Translational Plasmids |
Zdroj: | Biochemical and Biophysical Research Communications. 314:586-596 |
ISSN: | 0006-291X |
Popis: | Peroxin 3 (Pex3p) has been identified and characterized as a peroxisomal membrane protein in yeasts and mammals. We identified two putative homologs in Arabidopsis (AtPex3p, forms 1 and 2), both with an identical cluster of positively charged amino acid residues (RKHRRK) immediately preceding one of the two predicted transmembrane domains (TMD1). In transiently transformed Arabidopsis and tobacco BY-2 suspension-cultured cells, epitope-tagged AtPex3p (form 2) sorted post-translationally from the cytosol directly to peroxisomes, the first sorting pathway described for any peroxin in plants. TMD1 and RKHRRK were necessary for targeting form 2 to peroxisomes and sufficient for directing chloramphenicol acetyltransferase to peroxisomes in both cell types. The N and C termini of AtPex3p (form 2) extend into the peroxisomal matrix, different from mammal and yeast Pex3 proteins. Thus, two authentic peroxisomal membrane-bound Pex3p homologs possessing a membrane peroxisomal targeting signal, the first one defined for a plant peroxin and for any Pex3p homolog, exist in plant cells. |
Databáze: | OpenAIRE |
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