AthPEX10, a nuclear gene essential for peroxisome and storage organelle formation during Arabidopsis embryogenesis. Schumann, U., Wanner, G., Veenhuis, M., Schmid, M., & Gietl, C. Proceedings of the National Academy of Sciences of the United States of America, 100(16):9626–9631, August, 2003.
doi  abstract   bibtex   
In yeasts and mammals, PEX10 encodes an integral membrane protein with a C3HC4 RING finger motif in its C-terminal domain and is required for peroxisome biogenesis and matrix protein import. In humans, its dysfunction in peroxisome biogenesis leads to severe Zellweger Syndrome and infantile Refsum disease. Here we show that dysfunction of a homologous gene in Arabidopsis leads to lethality at the heart stage of embryogenesis, impairing the biogenesis of peroxisomes, lipid bodies, and protein bodies. In a T-DNA insertion mutant disrupting the fourth exon of the AthPEX10 gene, ultrastructural analyses fail to detect peroxisomes characteristic for wild-type embryogenesis. Storage triacyl glycerides are not assembled into lipid bodies (oil bodies; oleosomes) surrounded by the phospholipid-protein monolayer membrane. Instead, the dysfunctional monolayer membranes, which derive from the bilayer membrane of the endoplasmic reticulum, accumulate in the cytosol. Concomitantly the transfer of the storage proteins from their site of synthesis at the endoplasmic reticulum to the vacuoles is disturbed. The mutant can be rescued by transformation with wild-type AthPEX10 cDNA. Transformants of wild-type Hansenula polymorpha cells with the AthPEX10 cDNA did produce the encoded protein without targeting it to peroxisomes. Additionally, the cDNA could not complement a Hansenula pex10 mutant unable to form peroxisomes. The ultrastructural knockout phenotype of AthPEX10p suggests that this protein in Arabidopsis is essential for peroxisome, oleosome, and protein transport vesicle formation.
@article{schumann_athpex10_2003,
	title = {{AthPEX10}, a nuclear gene essential for peroxisome and storage organelle formation during {Arabidopsis} embryogenesis},
	volume = {100},
	issn = {0027-8424},
	doi = {10/dzx29q},
	abstract = {In yeasts and mammals, PEX10 encodes an integral membrane protein with a C3HC4 RING finger motif in its C-terminal domain and is required for peroxisome biogenesis and matrix protein import. In humans, its dysfunction in peroxisome biogenesis leads to severe Zellweger Syndrome and infantile Refsum disease. Here we show that dysfunction of a homologous gene in Arabidopsis leads to lethality at the heart stage of embryogenesis, impairing the biogenesis of peroxisomes, lipid bodies, and protein bodies. In a T-DNA insertion mutant disrupting the fourth exon of the AthPEX10 gene, ultrastructural analyses fail to detect peroxisomes characteristic for wild-type embryogenesis. Storage triacyl glycerides are not assembled into lipid bodies (oil bodies; oleosomes) surrounded by the phospholipid-protein monolayer membrane. Instead, the dysfunctional monolayer membranes, which derive from the bilayer membrane of the endoplasmic reticulum, accumulate in the cytosol. Concomitantly the transfer of the storage proteins from their site of synthesis at the endoplasmic reticulum to the vacuoles is disturbed. The mutant can be rescued by transformation with wild-type AthPEX10 cDNA. Transformants of wild-type Hansenula polymorpha cells with the AthPEX10 cDNA did produce the encoded protein without targeting it to peroxisomes. Additionally, the cDNA could not complement a Hansenula pex10 mutant unable to form peroxisomes. The ultrastructural knockout phenotype of AthPEX10p suggests that this protein in Arabidopsis is essential for peroxisome, oleosome, and protein transport vesicle formation.},
	language = {eng},
	number = {16},
	journal = {Proceedings of the National Academy of Sciences of the United States of America},
	author = {Schumann, Uwe and Wanner, Gerhard and Veenhuis, Marten and Schmid, Markus and Gietl, Christine},
	month = aug,
	year = {2003},
	pmid = {12883010},
	pmcid = {PMC170968},
	keywords = {Amino Acid Sequence, Arabidopsis, Arabidopsis Proteins, Carrier Proteins, Cell Membrane, Cell Nucleus, Cytosol, DNA, Complementary, Endoplasmic Reticulum, Exons, Lipid Bilayers, Lipid Metabolism, Membrane Transport Proteins, Microscopy, Electron, Molecular Sequence Data, Mutation, Organelles, Peroxins, Peroxisomes, Phospholipids, Plants, Genetically Modified, Protein Structure, Tertiary, Receptors, Cytoplasmic and Nuclear},
	pages = {9626--9631},
}
Downloads: 0
About
Documentation
Keywords
Search
Users
Terms and Conditions of Use
Privacy Policy
Sitemap
© BibBase.org 2021