RRC ID 11406
著者 Prestele J, Hierl G, Scherling C, Hetkamp S, Schwechheimer C, Isono E, Weckwerth W, Wanner G, Gietl C.
タイトル Different functions of the C3HC4 zinc RING finger peroxins PEX10, PEX2, and PEX12 in peroxisome formation and matrix protein import.
ジャーナル Proc Natl Acad Sci U S A
Abstract The integral peroxisomal membrane proteins PEX10, PEX2, and PEX12 contain a zinc RING finger close to the C terminus. Loss of function of these peroxins causes embryo lethality at the heart stage in Arabidopsis. Preventing the coordination of Zn(2+) ions by amino acid substitutions in PEX10, PEX2, and PEX12 and overexpressing the resulting conditional sublethal mutations in WT uncovered additional functions of PEX10. Plants overexpressing DeltaZn-mutant PEX10 display deformed peroxisomal shapes causing diminished contact with chloroplasts and possibly with mitochondria. These changes correlated with impaired metabolite transfer and, at high CO(2), recoverable defective photorespiration plus dwarfish phenotype. The N-terminal PEX10 domain is critical for peroxisome biogenesis and plant development. A point mutation in the highly conserved TLGEEY motif results in vermiform peroxisome shape without impairing organelle contact. Addition of an N-terminal T7 tag to WT PEX0 resulted in partially recoverable reduced growth and defective inflorescences persisting under high CO(2). In contrast, plants overexpressing PEX2-DeltaZn-T7 grow like WT in normal atmosphere, contain normal-shaped peroxisomes, but display impaired peroxisomal matrix protein import. PEX12-DeltaZn-T7 mutants exhibit unimpaired import of matrix protein and normal-shaped peroxisomes when grown in normal atmosphere. During seed germination, glyoxysomes form a reticulum around the lipid bodies for mobilization of storage oil. The formation of this glyoxysomal reticulum seemed to be impaired in PEX10-DeltaZn but not in PEX2-DeltaZn-T7 or PEX12-DeltaZn-T7 plants. Both cytosolic PEX10 domains seem essential for peroxisome structure but differ in metabolic function, suggesting a role for this plant peroxin in addition to the import of matrix protein via ubiquitination of PEX5.
巻・号 107(33)
ページ 14915-20
公開日 2010-8-17
DOI 10.1073/pnas.1009174107
PII 1009174107
PMID 20679226
PMC PMC2930433
MeSH Amino Acid Motifs / genetics Amino Acid Sequence Arabidopsis / genetics Arabidopsis / metabolism* Arabidopsis Proteins / genetics Arabidopsis Proteins / metabolism* Biological Transport Carbon Dioxide / metabolism Extracellular Matrix Proteins / metabolism Gene Expression Regulation, Plant Glyoxysomes / metabolism Glyoxysomes / ultrastructure Green Fluorescent Proteins / genetics Green Fluorescent Proteins / metabolism Membrane Proteins / genetics Membrane Proteins / metabolism* Membrane Transport Proteins / genetics Membrane Transport Proteins / metabolism* Metabolomics / methods Microscopy, Confocal Microscopy, Electron Models, Biological Molecular Sequence Data Mutation Peroxins Peroxisome-Targeting Signal 1 Receptor Peroxisomes / metabolism* Peroxisomes / ultrastructure Photosynthesis Plants, Genetically Modified RING Finger Domains / genetics Receptors, Cytoplasmic and Nuclear / genetics Receptors, Cytoplasmic and Nuclear / metabolism Reverse Transcriptase Polymerase Chain Reaction Sequence Homology, Amino Acid Zinc Fingers / genetics
IF 9.412
引用数 36
WOS 分野 MULTIDISCIPLINARY SCIENCES
リソース情報
シロイヌナズナ / 植物培養細胞・遺伝子 pda05805 pda10680