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Characterization of a CLE processing activity.
- Source :
-
Plant molecular biology [Plant Mol Biol] 2011 Jan; Vol. 75 (1-2), pp. 67-75. Date of Electronic Publication: 2010 Nov 04. - Publication Year :
- 2011
-
Abstract
- Proteins containing a conserved motif known as the CLE domain are found widely distributed across land plants. While the functions of most CLE proteins are unknown, specific CLE proteins have been shown to control shoot meristem, root and vascular development. This has been best studied for CLV3 which is required for stem cell differentiation at shoot and flower meristems. In vivo evidence indicates that the CLE domain is the functional region for CLV3, and that it is proteolytically processed from the CLV3 precursor protein. But the mechanism and activity responsible for this processing is poorly understood. Here we extend analysis of an in vitro CLE processing activity and show that in vitro cleavage occurs at Arg70, exactly matching in vivo maturation. We provide evidence that related processing activities are present in multiple tissues and species. We show that efficient protease recognition can occur with as little as four residues upstream of the CLE domain, and that the conserved arginine at position +1 and conserved acidic residues at positions -2 and/or -3 are required for efficient cleavage. Finally, we provide evidence that the N-terminal processing enzyme is a secreted serine protease while C-terminal processing may occur via a progressive carboxypeptidase.
- Subjects :
- Amino Acid Sequence
Arabidopsis Proteins genetics
Arginine genetics
Arginine metabolism
Binding Sites
Brassica chemistry
Carboxypeptidases metabolism
Cells, Cultured
Glutathione Transferase genetics
Glutathione Transferase metabolism
Hydrogen-Ion Concentration
Immunoblotting
Leucine analogs & derivatives
Leucine metabolism
Mass Spectrometry
Molecular Sequence Data
Plant Leaves metabolism
Plant Proteins metabolism
Plant Roots metabolism
Protein Precursors genetics
Recombinant Fusion Proteins genetics
Recombinant Fusion Proteins metabolism
Nicotiana cytology
Nicotiana metabolism
Arabidopsis Proteins metabolism
Protease Inhibitors metabolism
Protein Precursors metabolism
Serine Proteases metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 1573-5028
- Volume :
- 75
- Issue :
- 1-2
- Database :
- MEDLINE
- Journal :
- Plant molecular biology
- Publication Type :
- Academic Journal
- Accession number :
- 21052783
- Full Text :
- https://doi.org/10.1007/s11103-010-9708-2