|
rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:issue |
52
|
|
pubmed:dateCreated |
2004-12-21
|
|
pubmed:databankReference |
|
|
pubmed:abstractText |
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.
|
|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Dec
|
|
pubmed:issn |
0021-9258
|
|
pubmed:author |
|
|
pubmed:issnType |
Print
|
|
pubmed:day |
24
|
|
pubmed:volume |
279
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
54264-74
|
|
pubmed:dateRevised |
2009-9-3
|
|
pubmed:meshHeading |
pubmed-meshheading:15498773-Adenosine Triphosphatases,
pubmed-meshheading:15498773-Amino Acid Sequence,
pubmed-meshheading:15498773-Animals,
pubmed-meshheading:15498773-Arabidopsis,
pubmed-meshheading:15498773-Arabidopsis Proteins,
pubmed-meshheading:15498773-Binding Sites,
pubmed-meshheading:15498773-Carrier Proteins,
pubmed-meshheading:15498773-Cell Cycle Proteins,
pubmed-meshheading:15498773-Chromatography, Affinity,
pubmed-meshheading:15498773-Escherichia coli,
pubmed-meshheading:15498773-Gene Expression,
pubmed-meshheading:15498773-Immunoblotting,
pubmed-meshheading:15498773-Kinetics,
pubmed-meshheading:15498773-Mice,
pubmed-meshheading:15498773-Molecular Sequence Data,
pubmed-meshheading:15498773-Molecular Structure,
pubmed-meshheading:15498773-Mutagenesis,
pubmed-meshheading:15498773-Peptide Fragments,
pubmed-meshheading:15498773-Plant Roots,
pubmed-meshheading:15498773-Polymerase Chain Reaction,
pubmed-meshheading:15498773-Recombinant Fusion Proteins,
pubmed-meshheading:15498773-Seeds,
pubmed-meshheading:15498773-Sequence Alignment,
pubmed-meshheading:15498773-Spectrometry, Mass, Matrix-Assisted Laser...,
pubmed-meshheading:15498773-Structure-Activity Relationship
|
|
pubmed:year |
2004
|
|
pubmed:articleTitle |
Plant UBX domain-containing protein 1, PUX1, regulates the oligomeric structure and activity of arabidopsis CDC48.
|
|
pubmed:affiliation |
Department of Biochemistry, University of Wisconsin-Madison, Madison, Wisconsin 53706, USA.
|
|
pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.
|
