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 |