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A conserved dibasic site is essential for correct processing of the peptide hormone AtRALF1 in Arabidopsis thaliana
- Source :
- FEBS Letters. 582:3343-3347
- Publication Year :
- 2008
- Publisher :
- Wiley, 2008.
-
Abstract
- Prohormone proteins in animals and yeast are typically processed at dibasic sites by convertases. Propeptide hormones are also found in plants but little is known about processing. We show for the first time that a dibasic site upstream of a plant peptide hormone, AtRALF1, is essential for processing. Overexpression of preproAtRALF1 causes semi-dwarfism whereas overexpression of preproAtRALF1(R69A), the propeptide with a mutation in the dibasic site, shows a normal phenotype. RALF1(R69A) plants accumulate only the mutated proprotein and not the processed peptide. In vitro processing using microsomal fractions suggests that processing is carried out by a kexin-like convertase.
- Subjects :
- Peptide Hormones
Molecular Sequence Data
Prohormone
Arabidopsis
Biophysics
Peptide
Biology
Peptide hormone
Arginine
Cell Fractionation
Protein processing
Plant Roots
Biochemistry
Transformation, Genetic
Structural Biology
Microsomes
Genetics
medicine
Arabidopsis thaliana
Amino Acid Sequence
Proprotein
Protein precursor
Molecular Biology
Conserved Sequence
Convertase
chemistry.chemical_classification
Dibasic acid
Arabidopsis Proteins
Plant peptide hormone
Cell Biology
Plants, Genetically Modified
biology.organism_classification
Plant Leaves
chemistry
Mutation
medicine.drug
Subjects
Details
- ISSN :
- 00145793
- Volume :
- 582
- Database :
- OpenAIRE
- Journal :
- FEBS Letters
- Accession number :
- edsair.doi.dedup.....5494f00c347d8ca1077891f21b65315e