Plant UBX domain-containing protein 1, PUX1, regulates the oligomeric structure and activity of arabidopsis CDC48.

p97/CDC48 is a highly abundant hexameric AAA-ATPase that functions as a molecular chaperone in numerous diverse cellular activities. We have identified an Arabidopsis UBX domain-containing protein, PUX1, which functions to regulate the oligomeric structure of the Arabidopsis homolog of p97/CDC48, AtCDC48, as well as mammalian p97. PUX1 is a soluble ...
protein that co-fractionates with non-hexameric AtCDC48 and physically interacts with AtCDC48 in vivo. Binding of PUX1 to AtCDC48 is mediated through the UBX-containing C-terminal domain. However, disassembly of the chaperone is dependent upon the N-terminal domain of PUX1. These findings provide evidence that the assembly and disassembly of the hexameric p97/CDC48 complex is a dynamic process. This new unexpected level of regulation for p97/CDC48 was demonstrated to be critical in vivo as pux1 loss-of-function mutants display accelerated growth relative to wild-type plants. These results suggest a role for AtCDC48 and PUX1 in regulating plant growth.
Mesh Terms:
Adenosine Triphosphatases, Amino Acid Sequence, Animals, Arabidopsis, Arabidopsis Proteins, Binding Sites, Carrier Proteins, Cell Cycle Proteins, Chromatography, Affinity, Escherichia coli, Gene Expression, Immunoblotting, Kinetics, Mice, Molecular Sequence Data, Molecular Structure, Mutagenesis, Peptide Fragments, Plant Roots, Polymerase Chain Reaction, Recombinant Fusion Proteins, Seeds, Sequence Alignment, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization, Structure-Activity Relationship
J. Biol. Chem.
Date: Dec. 24, 2004
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