The Early-Acting Peroxin PEX19 Is Redundantly Encoded, Farnesylated, and Essential for Viability in Arabidopsis thaliana

Autor: Lucia C. Strader, Jerrad M. Stoddard, Sarah E. Burkhart, Zachary J. Wright, Bonnie Bartel, Margaret M. McDonnell
Rok vydání: 2015
Předmět:
0301 basic medicine
Mutant
Cell Membranes
Arabidopsis
lcsh:Medicine
Peroxin
Plant Science
Endoplasmic Reticulum
Biochemistry
Peroxins
Gene Expression Regulation
Plant
Genes
Reporter
Protein Isoforms
lcsh:Science
Phylogeny
Multidisciplinary
Plant Biochemistry
Chemical Reactions
Peroxisome
Plants
Cell biology
Chemistry
Seeds
Physical Sciences
Cellular Structures and Organelles
Research Article
Plant Somatic Embryogenesis Techniques
Arabidopsis Thaliana
Molecular Sequence Data
Immunoblotting
Protein Prenylation
Molecular Probe Techniques
Brassica
Biology
Research and Analysis Methods
03 medical and health sciences
Model Organisms
Bacterial Proteins
Plant and Algal Models
Peroxisomes
Amino Acid Sequence
Molecular Biology Techniques
Molecular Biology
Prenylation
Peroxisomal matrix
Arabidopsis Proteins
Endoplasmic reticulum
lcsh:R
Organisms
Fungi
Membrane Proteins
Biology and Life Sciences
Cell Biology
biology.organism_classification
Molecular biology
Yeast
Luminescent Proteins
030104 developmental biology
Membrane protein
Seedlings
Mutation
Protein prenylation
lcsh:Q
Genes
Lethal
Protein Processing
Post-Translational
Sequence Alignment
Zdroj: PLoS ONE
PLoS ONE, Vol 11, Iss 1, p e0148335 (2016)
ISSN: 1932-6203
Popis: Peroxisomes are single-membrane bound organelles that are essential for normal development in plants and animals. In mammals and yeast, the peroxin (PEX) proteins PEX3 and PEX19 facilitate the early steps of peroxisome membrane protein (PMP) insertion and pre-peroxisome budding from the endoplasmic reticulum. The PEX3 membrane protein acts as a docking site for PEX19, a cytosolic chaperone for PMPs that delivers PMPs to the endoplasmic reticulum or peroxisomal membrane. PEX19 is farnesylated in yeast and mammals, and we used immunoblotting with prenylation mutants to show that PEX19 also is fully farnesylated in wild-type Arabidopsis thaliana plants. We examined insertional alleles disrupting either of the two Arabidopsis PEX19 isoforms, PEX19A or PEX19B, and detected similar levels of PEX19 protein in the pex19a-1 mutant and wild type; however, PEX19 protein was nearly undetectable in the pex19b-1 mutant. Despite the reduction in PEX19 levels in pex19b-1, both pex19a-1 and pex19b-1 single mutants lacked notable peroxisomal β-oxidation defects and displayed normal levels and localization of peroxisomal matrix and membrane proteins. The pex19a-1 pex19b-1 double mutant was embryo lethal, indicating a redundantly encoded critical role for PEX19 during embryogenesis. Expressing YFP-tagged versions of either PEX19 isoform rescued this lethality, confirming that PEX19A and PEX19B act redundantly in Arabidopsis. We observed that pex19b-1 enhanced peroxisome-related defects of a subset of peroxin-defective mutants, supporting a role for PEX19 in peroxisome function. Together, our data indicate that Arabidopsis PEX19 promotes peroxisome function and is essential for viability.
Databáze: OpenAIRE
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